diff --git a/ruslan/DOI2META/Task_18_prepare_a_pipeline_to_pull_data_about_publications.ipynb b/ruslan/DOI2META/Task_18_prepare_a_pipeline_to_pull_data_about_publications.ipynb
new file mode 100644
index 0000000..ea607ac
--- /dev/null
+++ b/ruslan/DOI2META/Task_18_prepare_a_pipeline_to_pull_data_about_publications.ipynb
@@ -0,0 +1,350 @@
+{
+ "nbformat": 4,
+ "nbformat_minor": 0,
+ "metadata": {
+ "colab": {
+ "provenance": []
+ },
+ "kernelspec": {
+ "name": "python3",
+ "display_name": "Python 3"
+ },
+ "language_info": {
+ "name": "python"
+ }
+ },
+ "cells": [
+ {
+ "cell_type": "code",
+ "execution_count": null,
+ "metadata": {
+ "colab": {
+ "base_uri": "https://localhost:8080/"
+ },
+ "id": "URaGvJWXCSPH",
+ "outputId": "e521ecc0-3dd4-4650-fdfd-edf5274cd18c"
+ },
+ "outputs": [
+ {
+ "output_type": "stream",
+ "name": "stdout",
+ "text": [
+ "Requirement already satisfied: requests in /usr/local/lib/python3.11/dist-packages (2.32.3)\n",
+ "Requirement already satisfied: charset-normalizer<4,>=2 in /usr/local/lib/python3.11/dist-packages (from requests) (3.4.1)\n",
+ "Requirement already satisfied: idna<4,>=2.5 in /usr/local/lib/python3.11/dist-packages (from requests) (3.10)\n",
+ "Requirement already satisfied: urllib3<3,>=1.21.1 in /usr/local/lib/python3.11/dist-packages (from requests) (2.3.0)\n",
+ "Requirement already satisfied: certifi>=2017.4.17 in /usr/local/lib/python3.11/dist-packages (from requests) (2024.12.14)\n"
+ ]
+ }
+ ],
+ "source": [
+ "pip install requests"
+ ]
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "pip install biopython"
+ ],
+ "metadata": {
+ "colab": {
+ "base_uri": "https://localhost:8080/"
+ },
+ "id": "jgO7mM4FHfZ7",
+ "outputId": "7c219e20-71a5-48b6-abb9-21346f089fde"
+ },
+ "execution_count": null,
+ "outputs": [
+ {
+ "output_type": "stream",
+ "name": "stdout",
+ "text": [
+ "Requirement already satisfied: biopython in /usr/local/lib/python3.11/dist-packages (1.85)\n",
+ "Requirement already satisfied: numpy in /usr/local/lib/python3.11/dist-packages (from biopython) (1.26.4)\n"
+ ]
+ }
+ ]
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "pip install odfpy"
+ ],
+ "metadata": {
+ "colab": {
+ "base_uri": "https://localhost:8080/"
+ },
+ "id": "B9GVsFTnfV01",
+ "outputId": "3d359ad3-3a53-4cee-ef11-d44c2342c41c"
+ },
+ "execution_count": null,
+ "outputs": [
+ {
+ "output_type": "stream",
+ "name": "stdout",
+ "text": [
+ "Requirement already satisfied: odfpy in /usr/local/lib/python3.11/dist-packages (1.4.1)\n",
+ "Requirement already satisfied: defusedxml in /usr/local/lib/python3.11/dist-packages (from odfpy) (0.7.1)\n"
+ ]
+ }
+ ]
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "!wget -O \"openTECR recuration.ods\" \"https://docs.google.com/spreadsheets/d/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c/export?format=ods\""
+ ],
+ "metadata": {
+ "colab": {
+ "base_uri": "https://localhost:8080/"
+ },
+ "id": "3b9q8AZgezQq",
+ "outputId": "c0d01a92-2a35-4588-d16e-b6e84c27e431"
+ },
+ "execution_count": null,
+ "outputs": [
+ {
+ "output_type": "stream",
+ "name": "stdout",
+ "text": [
+ "--2025-01-19 09:11:24-- https://docs.google.com/spreadsheets/d/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c/export?format=ods\n",
+ "Resolving docs.google.com (docs.google.com)... 142.251.179.100, 142.251.179.138, 142.251.179.101, ...\n",
+ "Connecting to docs.google.com (docs.google.com)|142.251.179.100|:443... connected.\n",
+ "HTTP request sent, awaiting response... 307 Temporary Redirect\n",
+ "Location: https://doc-00-8k-sheets.googleusercontent.com/export/54bogvaave6cua4cdnls17ksc4/q2h8j528ksl67k4dceiprkoqoc/1737277880000/115120384215235060766/*/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c?format=ods [following]\n",
+ "Warning: wildcards not supported in HTTP.\n",
+ "--2025-01-19 09:11:24-- https://doc-00-8k-sheets.googleusercontent.com/export/54bogvaave6cua4cdnls17ksc4/q2h8j528ksl67k4dceiprkoqoc/1737277880000/115120384215235060766/*/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c?format=ods\n",
+ "Resolving doc-00-8k-sheets.googleusercontent.com (doc-00-8k-sheets.googleusercontent.com)... 172.253.115.132, 2607:f8b0:4004:c06::84\n",
+ "Connecting to doc-00-8k-sheets.googleusercontent.com (doc-00-8k-sheets.googleusercontent.com)|172.253.115.132|:443... connected.\n",
+ "HTTP request sent, awaiting response... 200 OK\n",
+ "Length: unspecified [application/vnd.oasis.opendocument.spreadsheet]\n",
+ "Saving to: ‘openTECR recuration.ods’\n",
+ "\n",
+ "openTECR recuration [ <=> ] 2.43M --.-KB/s in 0.07s \n",
+ "\n",
+ "2025-01-19 09:11:47 (36.2 MB/s) - ‘openTECR recuration.ods’ saved [2549105]\n",
+ "\n"
+ ]
+ }
+ ]
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "import pandas as pd\n",
+ "from Bio import Entrez\n",
+ "import numpy as np\n",
+ "import time\n",
+ "\n",
+ "def crossref(doi):\n",
+ " url = f\"https://api.crossref.org/works/{doi}\"\n",
+ " response = requests.get(url)\n",
+ " if response.status_code == 200:\n",
+ " return response.json()\n",
+ " else:\n",
+ " return {\"error\": f\"DOI not found in CrossRef: {doi}\"}\n",
+ "\n",
+ "def pubmed(pmid):\n",
+ " handle = Entrez.efetch(db=\"pubmed\", id=pmid, retmode=\"xml\")\n",
+ " response = Entrez.read(handle)\n",
+ " handle.close()\n",
+ " return response\n",
+ "\n",
+ "def doires2meta(response):\n",
+ " metadata = {}\n",
+ " metadata['Title'] = response['message']['title']\n",
+ " date = response['message']['created']['date-parts'][0]\n",
+ " metadata['Date'] = f'{date[2]}.{date[1]}.{date[0]}'\n",
+ " metadata['Publisher'] = response['message']['publisher']\n",
+ " metadata['License'] = response['message']['license'][0]['URL']\n",
+ " metadata['Type'] = response['message']['type']\n",
+ " metadata['Volume'] = response['message']['volume']\n",
+ " metadata['Issue'] = response['message']['issue']\n",
+ " metadata['Page'] = response['message']['page']\n",
+ " fn = []\n",
+ " sn = []\n",
+ " for b in response['message']['author']:\n",
+ " fn.append(b['given'])\n",
+ " sn.append(b['family'])\n",
+ "\n",
+ " string = ''\n",
+ "\n",
+ " for i in range(len(fn)):\n",
+ " string = string + fn[i] + \" \" + sn[i] + \", \"\n",
+ "\n",
+ " string = string[:-2]\n",
+ " metadata['Authors'] = string\n",
+ " metadata['Language'] = response['message']['language']\n",
+ " return metadata\n",
+ "\n",
+ "def pubmed2meta(response):\n",
+ " metadata = {}\n",
+ " try:\n",
+ " metadata['Language'] = response['PubmedArticle'][0]['MedlineCitation']['Article']['Language']\n",
+ " except:\n",
+ " metadata['Language'] = '-'\n",
+ " try:\n",
+ " metadata['Volume'] = response['PubmedArticle'][0]['MedlineCitation']['Article']['Journal']['JournalIssue']['Volume']\n",
+ " except:\n",
+ " metadata['Volume'] = '-'\n",
+ " try:\n",
+ " metadata['Issue'] = response['PubmedArticle'][0]['MedlineCitation']['Article']['Journal']['JournalIssue']['Issue']\n",
+ " except:\n",
+ " metadata['Issue'] = \"-\"\n",
+ " try:\n",
+ " metadata['Page'] = response['PubmedArticle'][0]['MedlineCitation']['Article']['Pagination']['MedlinePgn']\n",
+ " except:\n",
+ " metadata['Page'] = \"-\"\n",
+ " date = response['PubmedArticle'][0]['MedlineCitation']['Article']['Journal']['JournalIssue']['PubDate']\n",
+ " try:\n",
+ " metadata['Journal'] = response['PubmedArticle'][0]['MedlineCitation']['Article']['Journal']['Title']\n",
+ " except:\n",
+ " metadata['Journal'] = \"-\"\n",
+ " try:\n",
+ " metadata['Abstract'] = response['PubmedArticle'][0]['MedlineCitation']['Article']['Abstract']['AbstractText'][0]\n",
+ " except:\n",
+ " metadata['Abstract'] = '-'\n",
+ " #print(date)\n",
+ " try:\n",
+ " month = date['Month']\n",
+ " except:\n",
+ " month = ' '\n",
+ " year = date['Year']\n",
+ " metadata['Date'] = f'{month} {year}'\n",
+ " try:\n",
+ " fn = []\n",
+ " sn = []\n",
+ " for b in response['PubmedArticle'][0]['MedlineCitation']['Article']['AuthorList']:\n",
+ " fn.append(b['ForeName'])\n",
+ " sn.append(b['LastName'])\n",
+ "\n",
+ " string = ''\n",
+ "\n",
+ " for i in range(len(fn)):\n",
+ " string = string + fn[i] + \" \" + sn[i] + \", \"\n",
+ "\n",
+ " string = string[:-2]\n",
+ " metadata['Authors'] = string\n",
+ " except:\n",
+ " metadata['Authors'] = \"-\"\n",
+ " return metadata\n",
+ "\n",
+ "def return_blank(indi):\n",
+ " metadata = {}\n",
+ " if indi == \"pub\":\n",
+ " metadata['Language'] = '-'\n",
+ " metadata['Volume'] = '-'\n",
+ " metadata['Issue'] = '-'\n",
+ " metadata['Page'] = '-'\n",
+ " metadata['Journal'] = '-'\n",
+ " metadata['Abstract'] = '-'\n",
+ " metadata['Date'] = '-'\n",
+ " metadata['Authors'] = '-'\n",
+ " if indi == \"doi\":\n",
+ " metadata['Title'] = '-'\n",
+ " metadata['Language'] = '-'\n",
+ " metadata['Volume'] = '-'\n",
+ " metadata['Issue'] = '-'\n",
+ " metadata['Page'] = '-'\n",
+ " metadata['Publisher'] = '-'\n",
+ " metadata['Date'] = '-'\n",
+ " metadata['Authors'] = '-'\n",
+ " metadata['License'] = '-'\n",
+ " metadata['Type'] = '-'\n",
+ " return metadata"
+ ],
+ "metadata": {
+ "id": "un4HAXdiGVSB"
+ },
+ "execution_count": null,
+ "outputs": []
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "Entrez.email = \"ruslanibragimovut@outlook.com\"\n",
+ "df = pd.read_excel(\"openTECR recuration.ods\", sheet_name=\"references\")\n",
+ "pmids = df['pmid'].to_list()\n",
+ "dois = df['doi'].to_list()\n"
+ ],
+ "metadata": {
+ "id": "8YsLraZn6JKK"
+ },
+ "execution_count": null,
+ "outputs": []
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "doismeta = []\n",
+ "for d in dois:\n",
+ " if type(d) == type('Is a string?'):\n",
+ " r = crossref(d)\n",
+ " #print(r)\n",
+ "\n",
+ " try:\n",
+ " d = doires2meta(r)\n",
+ " except:\n",
+ " d = return_blank('doi')\n",
+ "\n",
+ " doismeta.append(d)\n",
+ " else:\n",
+ " c = return_blank('doi')\n",
+ " doismeta.append(c)"
+ ],
+ "metadata": {
+ "collapsed": true,
+ "id": "Nx273Y9i_qpF"
+ },
+ "execution_count": null,
+ "outputs": []
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "pmidsmeta = []\n",
+ "for pmid in pmids:\n",
+ " if np.isnan(pmid) == False:\n",
+ " time.sleep(1)\n",
+ " r = pubmed(str(pmid))\n",
+ " #print(r)\n",
+ " d = pubmed2meta(r)\n",
+ " pmidsmeta.append(d)\n",
+ " else:\n",
+ " c = return_blank('pub')\n",
+ " pmidsmeta.append(c)"
+ ],
+ "metadata": {
+ "id": "XhQRgqi11jVy"
+ },
+ "execution_count": null,
+ "outputs": []
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "dfpub = pd.DataFrame(pmidsmeta)\n",
+ "dfdoi = pd.DataFrame(doismeta)"
+ ],
+ "metadata": {
+ "id": "UIRdf5jcKqmD"
+ },
+ "execution_count": null,
+ "outputs": []
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "dfpubC = pd.concat([df, dfpub], axis=1)\n",
+ "dfdoiC = pd.concat([df, dfdoi], axis=1)\n",
+ "dfpubC.to_csv('openTECRmetadataPubMed.csv')\n",
+ "dfdoiC.to_csv('openTECRmetadataDOI.csv')"
+ ],
+ "metadata": {
+ "id": "L7zvwcIHLins"
+ },
+ "execution_count": null,
+ "outputs": []
+ }
+ ]
+}
\ No newline at end of file
diff --git a/ruslan/DOI2META/openTECRmetadataDOI.csv b/ruslan/DOI2META/openTECRmetadataDOI.csv
new file mode 100644
index 0000000..11ac432
--- /dev/null
+++ b/ruslan/DOI2META/openTECRmetadataDOI.csv
@@ -0,0 +1,1072 @@
+,reference_code,pmid,doi,comment,Title,Date,Publisher,License,Type,Volume,Issue,Page,Authors,Language
+0,00BYR/GOL,10723544.0,10.1016/S0301-4622(99)00145-3,,['Thermodynamics of reactions catalyzed by anthranilate synthase'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,84,1,45-64,"W.Malcolm Byrnes, Robert N. Goldberg, Marcia J. Holden, Martin P. Mayhew, Yadu B. Tewari",en
+1,00DIC/BUR,10748184.0,10.1074/jbc.M910044199,"same as 01DIC/BUR, part 7, ref 98",['Determination of the Free-Energy Change for Repair of a DNA Phosphodiester Bond'],26.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,275,21,15828-15831,"Kirsten S. Dickson, Christopher M. Burns, John P. Richardson",en
+2,00DIE,,,"part 7, ref 150",-,-,-,-,-,-,-,-,-,-
+3,00FLO/SEW,10620267.0,10.1002/(SICI)1097-0290(20000205)67:3<364::AID-BIT13>3.0.CO,,-,-,-,-,-,-,-,-,-,-
+4,00FRA/KOS,,10.1039/b000018n,,-,-,-,-,-,-,-,-,-,-
+5,00KIS/TEW,,10.1006/jcht.1999.0496,,['A thermodynamic study of the hydrolysis of L-glutamine to (L-glutamate + ammonia) and of L-asparagine to (L -aspartate + ammonia)'],18.9.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,32,9,1077-1090,"Nand Kishore, Yadu B. Tewari, Robert N. Goldberg",en
+6,00LIA/HUA,,10.1016/S0040-6031(00)00355-5,,['Microcalorimetric studies on the creatine kinase-catalyzed reaction in the presence of guanidine hydrochloride'],26.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,348,1-2,41-47,"Yi Liang, Guo-Chang Huang, Jie Chen, Jun-Mei Zhou",en
+7,00LIA/QU,,10.1016/S0009-2509(00)00417-6,,['An on-line calorimetric study of the dismutation of superoxide anion catalyzed by SOD in batch reactors'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,55,24,6071-6078,"Yi Liang, Song-Sheng Qu, Cun-Xin Wang, Guo-Lin Zou, Yuan-Xin Wu, Ding-Huo Li",en
+8,00ROD/BAR,10890880.0,10.1073/pnas.120168097,,-,-,-,-,-,-,-,-,-,-
+9,00TEW,,10.1016/S1381-1177(99)00087-9,,['Thermodynamics of the lipase-catalyzed transesterification of (−)-menthol and dodecyl dodecanoate in organic solvents'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,9,1-3,83-90,Yadu B. Tewari,en
+10,00TEW/DAV,,10.1006/jcht.2000.0677,,['A thermodynamic study of the conversion of chorismate to isochorismate'],18.9.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,32,8,1057-1070,"Yadu B. Tewari,, Andrew M. Davis,, Prasad Reddy,, Robert N. Goldberg",en
+11,00TEW/GOL,,10.1006/jcht.2000.0686,,['Thermodynamics of reactions catalysed by branched-chain-amino-acid transaminase'],18.9.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,32,10,1381-1398,"Yadu B. Tewari, Robert N. Goldberg, J.David Rozzell",en
+12,00WU/FEN,,10.1021/ja992286h,,-,-,-,-,-,-,-,-,-,-
+13,00ZHE/BLA,10736170.0,10.1021/bi992676g,,-,-,-,-,-,-,-,-,-,-
+14,01TEW/BUN,,10.1016/S1381-1177(01)00016-9,,['Thermodynamics of the lipase-catalyzed esterification of glycerol and n-octanoic acid in organic solvents and in the neat reaction mixture'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,15,4-6,135-145,"Yadu B. Tewari, David M. Bunk",en
+15,01TEW/KIS,,10.1006/jcht.2001.0862,,['Thermochemistry of the reaction { phospho enol pyruvate(aq)+d -erythrose 4-phosphate(aq) + H2 O(l) = 2-dehydro-3-deoxy- d - arabino -heptonate 7-phosphate(aq) + phosphate(aq) }'],6.10.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,33,12,1791-1805,"Yadu B. Tewari, Nand Kishore, Ronald Bauerle, William R. LaCourse, Robert N. Goldberg",en
+16,01TIS/IHL,,,,-,-,-,-,-,-,-,-,-,-
+17,02DOB/HIT,11986306.0,10.1074/jbc.M111422200,,['Thermodynamics of the Pyruvate Kinase Reaction and the Reversal of Glycolysis in Heart and Skeletal Muscle'],28.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,277,30,27176-27182,"Geoffrey P. Dobson, Sam Hitchins, Walter E. Teague",en
+18,02FLO/HAL,12001171.0,10.1002/bit.10260,,['Full model for reversible kinetics of lipase‐catalyzed sugar–ester synthesis in 2‐methyl 2‐butanol'],25.8.2002,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,78,7,795-801,"Maria Victoria Flores, Peter J. Halling",en
+19,02ISO/KOI,,10.1016/S1389-1723(02)80173-6,,['Crystallization and some properties of d-lactate dehydrogenase from Staphylococcus sp. LDH-1'],17.6.2010,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,94,4,330-335,"Kimiyasu Isobe, Yoshinao Koide, Masaaki Yokoe, Norio Wakao",en
+20,02KIM/BAK,12107130.0,10.1128/JB.184.15.4134-4140.2002,,['The 2-Aminoethylphosphonate-Specific Transaminase of the 2-Aminoethylphosphonate Degradation Pathway'],28.7.2002,American Society for Microbiology,https://journals.asm.org/non-commercial-tdm-license,journal-article,184,15,4134-4140,"Alexander D. Kim, Angela S. Baker, Debra Dunaway-Mariano, W. W. Metcalf, B. L. Wanner, Brian M. Martin",en
+21,02NES/ZHO,12133002.0,10.1042/bj20020551,,-,-,-,-,-,-,-,-,-,-
+22,02TEW/HAW,,10.1016/S0021-9614(02)00226-4,,['A thermodynamic study of the reactions: {2-dehydro-3-deoxy-d-arabino-heptanoate 7-phosphate(aq)=3-dehydroquinate(aq) + phosphate(aq)} and {3-dehydroquinate(aq)=3-dehydroshikimate(aq)+H2O(l)}'],9.1.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,34,10,1671-1691,"Yadu B. Tewari, Robert N. Goldberg, Alastair R. Hawkins, Heather K. Lamb",en
+23,02VUO/PAS,,10.1080/10242420290029463,,-,-,-,-,-,-,-,-,-,-
+24,03BIA,12611889.0,10.1074/jbc.M211103200,,['Calorimetric Determination of Thermodynamic Parameters of Reaction Reveals Different Enthalpic Compensations of the Yeast Hexokinase Isozymes'],17.5.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,278,21,18709-18713,M. Lucia Bianconi,en
+25,03GOL/TEW,,10.1016/j.jct.2003.08.002,,"['Thermodynamics of the hydrolysis reactions of adenosine 3′,5′-(cyclic)phosphate(aq) and phosphoenolpyruvate(aq); the standard molar formation properties of 3′,5′-(cyclic)phosphate(aq) and phosphoenolpyruvate(aq)']",15.10.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,35,11,1809-1830,"Robert N Goldberg, Yadu B Tewari",en
+26,03KIN,12573288.0,10.1016/S0003-9861(02)00692-6,,['Thermodynamics of the reduction of NADP with 2-propanol catalyzed by an NADP-dependent alcohol dehydrogenase'],4.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,410,2,280-286,M. Todd King,en
+27,03KOB/FUR,,10.1016/S1381-1177(03)00109-7,,-,-,-,-,-,-,-,-,-,-
+28,03MER/WOO,12805358.0,10.1074/jbc.M303661200,,['Escherichia coli YrbH Is a D-Arabinose 5-Phosphate Isomerase'],22.8.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,278,35,32771-32777,"Timothy C. Meredith, Ronald W. Woodard",en
+29,03RAN/VAN,12568939.0,10.1016/S0301-4622(02)00254-5,,['Enzyme catalysis in microgravity: steady-state kinetic analysis of the isocitrate lyase reaction'],4.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,103,2,169-177,"Francesco Ranaldi, Paolo Vanni, Eugenio Giachetti",en
+30,03TEW/GOL,,10.1016/S0021-9614(03)00111-3,,['Thermodynamics of the oxidation–reduction reaction {2 glutathionered(aq)+NADPox(aq)=glutathioneox(aq)+NADPred(aq)}'],1.8.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,35,8,1361-1381,"Yadu B. Tewari, Robert N. Goldberg",en
+31,03TEW/VAN,,10.1016/S1381-1177(02)00120-0,,['Thermodynamics of the lipase-catalyzed transesterification of 1-phenyl-1-alkanols and butyl acetate in organic solvents'],10.12.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,21,3,123-131,"Yadu B Tewari, David J Vanderah, J.David Rozzell",en
+32,03WAT/YAM,,10.1016/S1381-1177(03)00102-4,,"['Occurrence of a unique amino acid racemase in a basidiomycetous mushroom, Lentinus edodes']",16.7.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,23,2-6,379-387,"Akira Watanabe, Shiro Yamaguchi, Koichiro Urabe, Yasuhiko Asada",en
+33,04DAS/BOM,15322117.0,10.1074/jbc.M408866200,,['Heat of PPi Hydrolysis Varies Depending on the Enzyme Used'],21.8.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,279,44,45613-45617,"Wagner S. da-Silva, Flavio M. Bomfim, Antonio Galina, Leopoldo de Meis",en
+34,04LI/LI,,10.1002/cjoc.20040220307,,['Kinetic Studies on Na+/K+‐ATPase by Using Thermokinetic Method'],8.9.2010,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,22,3,252-255,"Xia Li, Jie Li, Zhi‐Yong Wang, Xiu‐Yin Xie, Xi Yang, Cun‐Xin Wang",en
+35,04STO/SCH,15158492.0,10.1016/S0003-2697(04)00219-2,,['Importance of product/reactant equilibration in the kinetics of the phosphoglucose isomerization reaction by differential stopped flow microcalorimetry*1'],26.5.2004,Elsevier BV,http://www.elsevier.com/tdm/userlicense/1.0/,journal-article,329,2,307-315,M STODEMAN,en
+36,04TEW/IHA,,10.1016/j.molcatb.2004.04.005,,['A thermodynamic study of the lipase-catalyzed transesterification of benzyl alcohol and butyl acetate in supercritical carbon dioxide media'],3.6.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,30,3-4,131-136,"Yadu B Tewari, Toshihide Ihara, Karen W Phinney, Martin P Mayhew",en
+37,05SIR/HUE,,10.1016/j.tca.2004.06.011,,['Thermochemical investigations of hydrolysis of p-nitrophenyl acetate in water–acetontrile mixtures'],31.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,426,1-2,1-6,"Vladimir A. Sirotkin, Regina Huettl, Gert Wolf",en
+38,05TEW/GOL,,10.1016/j.jct.2004.11.011,,['Thermodynamics of the hydrolysis reactions of nitriles'],19.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,37,7,720-728,"Yadu B. Tewari, Robert N. Goldberg",en
+39,05TEW/SCH,,10.1016/j.jct.2004.08.002,,['A thermodynamic study of the ketoreductase-catalyzed reduction of 2-alkanones in non-aqueous solvents'],30.9.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,37,1,89-96,"Yadu B. Tewari, Michele M. Schantz, Karen W. Phinney, J. David Rozzell",en
+40,06AIR,16427818.0,10.1016/j.bbapap.2005.11.020,,['Analysis of the kinetic mechanism of arginyl-tRNA synthetase'],23.12.2005,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,1764,2,307-319,R. Kalervo Airas,en
+41,06MCC/ARA,16519510.0,10.1021/bi052232m,,-,-,-,-,-,-,-,-,-,-
+42,06ONO/YAN,16616264.0,10.1016/j.phytochem.2006.02.017,,['Alanine racemase of alfalfa seedlings (Medicago sativa L.): First evidence for the presence of an amino acid racemase in plants'],18.4.2006,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,67,9,856-860,"Kazutoshi Ono, Kazuki Yanagida, Tadao Oikawa, Tadashi Ogawa, Kenji Soda",en
+43,06POD/BEL,16884305.0,10.1021/jm060202r,,-,-,-,-,-,-,-,-,-,-
+44,06TAN/SUR,16967985.0,10.1021/ja0627702,,-,-,-,-,-,-,-,-,-,-
+45,06TEW/KIS,,10.1016/j.jct.2005.12.014,,['A thermodynamic study of ketoreductase-catalyzed reactions 3. Reduction of 1-phenyl-1-alkanones in non-aqueous solvents'],4.3.2006,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,38,10,1165-1171,"Yadu B. Tewari, Nand Kishore, J. David Rozzell, David J. Vanderah, Michele M. Schantz",en
+46,06TEW/PHI,,10.1016/j.jct.2005.06.005,,['A thermodynamic study of ketoreductase-catalyzed reactions 2. Reduction of cycloalkanones in non-aqueous solvents'],3.8.2005,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,38,4,388-395,"Yadu B. Tewari, Karen W. Phinney, Joel F. Liebman",en
+47,06XU/WES,17002315.0,10.1021/bi0610808,,-,-,-,-,-,-,-,-,-,-
+48,07LIN/ALG,17223711.0,10.1021/bi062067q,,-,-,-,-,-,-,-,-,-,-
+49,07TEW/KIS,,10.1016/j.jct.2006.10.010,,['Thermodynamics of reactions catalyzed by d-hydantoinase and N-carbamoyl-d-amino acid hydrolase'],29.10.2006,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,39,5,717-728,"Yadu B. Tewari, Nand Kishore, Brian E. Lang, Robert N. Goldberg",en
+50,07TEW/LIE,,10.1016/j.jct.2006.12.007,,['A thermodynamic study of ketoreductase-catalyzed reactions 4. Reduction of 2-substituted cyclohexanones in n-hexane'],20.12.2006,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,39,7,1090-1097,"Yadu B. Tewari, Joel F. Liebman, J. David Rozzell, David J. Vanderah, Michele M. Schantz",en
+51,26QUA/WOO,16743691.0,10.1042/bj0200545,,-,-,-,-,-,-,-,-,-,-
+52,29WOO,16744231.0,10.1042/bj0230472,,-,-,-,-,-,-,-,-,-,-
+53,31BOR/SCH,,10.1016/S0021-9258(17)32602-9,,"['THE FREE ENERGY, HEAT, AND ENTROPY OF FORMATION OF l-MALIC ACID']",18.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,92,3,559-567,"Henry Borsook, Hermann F. Schott",en
+54,34JAC,,,,-,-,-,-,-,-,-,-,-,-
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+63,35MEY/SCH,,,,-,-,-,-,-,-,-,-,-,-
+64,36EUL/ADL,,10.1515/bchm2.1936.241.6.239,,-,-,-,-,-,-,-,-,-,-
+65,36LEH,,,,-,-,-,-,-,-,-,-,-,-
+66,36MEY/LOH,,,,-,-,-,-,-,-,-,-,-,-
+67,36MEY/SCH,,,,-,-,-,-,-,-,-,-,-,-
+68,36VEI,,,,-,-,-,-,-,-,-,-,-,-
+69,37ADL/SRE,,10.1515/bchm2.1937.249.1.24,,-,-,-,-,-,-,-,-,-,-
+70,37EUL/ADL,,10.1515/bchm2.1937.247.1-2.65,,-,-,-,-,-,-,-,-,-,-
+71,37EUL/ADL2,,10.1515/bchm2.1937.249.1.1,,-,-,-,-,-,-,-,-,-,-
+72,37EUL/ADL3,,10.1515/bchm2.1937.245.5-6.217,,-,-,-,-,-,-,-,-,-,-
+73,37NEG/WUL,,,,-,-,-,-,-,-,-,-,-,-
+74,37STU,,10.1021/ja01287a037,,-,-,-,-,-,-,-,-,-,-
+75,38EUL/ADL,,10.1515/bchm2.1938.254.2.61,,-,-,-,-,-,-,-,-,-,-
+76,38MEY/SCH,,,,-,-,-,-,-,-,-,-,-,-
+77,38SCH/HEL,,10.1002/cber.19380710717,,['Desamino‐cozymase'],20.7.2007,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,71,7,1471-1479,"Fritz Schlenk, Harry Hellström, Hans v. Euler",en
+78,39COH,16747057.0,10.1042/bj0331478,,-,-,-,-,-,-,-,-,-,-
+79,40COH,,10.1016/S0021-9258(18)73021-4,,['KINETICS OF TRANSAMINASE ACTIVITY'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,136,3,585-601,Philip P. Cohen,en
+80,40HER/GOR,16747255.0,10.1042/bj0341108,,-,-,-,-,-,-,-,-,-,-
+81,40KRE/SMY,16747248.0,10.1042/bj0341041,,-,-,-,-,-,-,-,-,-,-
+82,41UTT/WER,16560478.0,10.1128/jb.42.5.665-676.1941,,['Occurrence of the Aldolase and Isomerase Equilibria in Bacterial Metabolism'],3.1.2020,American Society for Microbiology,https://journals.asm.org/non-commercial-tdm-license,journal-article,42,5,665-676,"M. F. Utter, C. H. Werkman",en
+83,41WAR/CHR,,,,-,-,-,-,-,-,-,-,-,-
+84,42COL/SUT,,10.1016/S0021-9258(18)72525-8,,['POLYSACCHARIDE SYNTHESIS FROM GLUCOSE BY MEANS OF PURIFIED ENZYMES'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,144,2,423-437,"Sidney P. Colowick, Earl W. Sutherland",en
+85,42LEN/STR,,,,-,-,-,-,-,-,-,-,-,-
+86,43BAN,,,,-,-,-,-,-,-,-,-,-,-
+87,43DOU,,10.1016/S0021-9258(18)44907-1,,['STUDIES ON THE PHOSPHOROLYSIS OF SUCROSE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,151,2,351-361,Michael Doudoroff,en
+88,43KAL,,10.1016/S0021-9258(18)72325-9,,['THE RÔLE OF MYOKINASE IN TRANSPHOSPHORYLATIONS'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,148,1,127-137,Herman M. Kalckar,en
+89,43KRE/EGG,16747647.0,10.1042/bj0370334,,-,-,-,-,-,-,-,-,-,-
+90,43KUB/OTT,,,,-,-,-,-,-,-,-,-,-,-
+91,43MEY/JUN,,10.1016/S0021-9258(18)72218-7,,"['THE EQUILIBRIA OF ISOMERASE AND ALDOLASE, AND THE PROBLEM OF THE PHOSPHORYLATION OF GLYCERALDEHYDE PHOSPHATE']",5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,149,1,71-92,"O. Meyerhof, R. Junowicz-Kocholaty",en
+92,44LIP,,10.1016/S0021-9258(18)43172-9,,['ENZYMATIC SYNTHESIS OF ACETYL PHOSPHATE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,155,1,55-70,Fritz Lipmann,en
+93,45DAR,,10.1111/j.1748-1716.1945.tb00300.x,,['Kinetic and Thermodynamic Investigations on the Transamination Process'],9.12.2008,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,10,2,150-161,SVEN DARLING,en
+94,45DRA/MEY,,10.1016/S0021-9258(18)51091-7,,['A SPECTROPHOTOMETRIC STUDY OF THE OXIDATION AND PHOSPHORYLATION OF d-GLYCERALDEHYDE 3-PHOSPHATE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,157,2,571-583,"David L. Drabkin, Otto Meyerhof",en
+95,45GRE/LEL,21006939.0,10.1016/S0021-9258(17)41491-8,,['TRANSAMINASES'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,161,2,559-582,"D.E. Green, Luis F. Leloir, V. Nocito",en
+96,45OHL,,10.1515/bchm2.1947.282.1-2.37,,-,-,-,-,-,-,-,-,-,-
+97,46OHL,,10.1515/zna-1946-0108,appears in part 3 and in part 4,['Wärmemessung bei Fermentreaktionen'],24.9.2019,Walter de Gruyter GmbH,http://creativecommons.org/licenses/by-nc-nd/3.0/,journal-article,1,1,30-35,Paul Ohlmeyer,en
+98,46OHL2,,10.1515/zna-1946-0107,appears in part 3,['Über Phosphatase'],11.6.2020,Walter de Gruyter GmbH,http://creativecommons.org/licenses/by-nc-nd/3.0/,journal-article,1,1,18-30,Paul Ohlmeyer,en
+99,47BUC,,10.1016/0006-3002(47)90143-1,,-,-,-,-,-,-,-,-,-,-
+100,47KAL,20285041.0,10.1016/S0021-9258(17)30999-7,,['DIFFERENTIAL SPECTROPHOTOMETRY OF PURINE COMPOUNDS BY MEANS OF SPECIFIC ENZYMES'],18.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,167,2,461-475,Herman M. Kalckar,en
+101,47MEY/OES,,10.1016/S0021-9258(17)34929-3,,['THE MECHANISM OF THE OXIDATIVE REACTION IN FERMENTATION'],18.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,170,1,1-22,"Otto Meyerhof, Peter Oesper",en
+102,48KOR,18098602.0,10.1016/S0021-9258(18)57167-2,,['THE PARTICIPATION OF INORGANIC PYROPHOSPHATE IN THE REVERSIBLE ENZYMATIC SYNTHESIS OF DIPHOSPHOPYRIDINE NUCLEOTIDE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,176,3,1475-1476,Arthur. Kornberg,en
+103,48OCH,18914071.0,10.1016/S0021-9258(18)57383-X,,['BIOSYNTHESIS OF TRICARBOXYLIC ACIDS BY CARBON DIOXIDE FIXATION'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,174,1,133-157,Severo Ochoa,en
+104,48SCO/POW,18909182.0,10.1021/ja01183a070,,-,-,-,-,-,-,-,-,-,-
+105,48SOR/DEG,,,,-,-,-,-,-,-,-,-,-,-
+106,49BAR,18135786.0,10.1016/S0021-9258(18)56670-9,,['CRYSTALLINE GLYCEROPHOSPHATE DEHYDROGENASE FROM RABBIT MUSCLE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,180,2,535-541,Tadeusz. Baranowski,en
+107,49HES,18135821.0,10.1016/S0021-9258(18)56708-9,,['ACYLATION REACTIONS MEDIATED BY PURIFIED ACETYLCHOLINE ESTERASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,180,2,879-881,Shlomo. Hestrin,en
+108,49MEY/GRE,18116987.0,10.1016/S0021-9258(18)56882-4,,['SYNTHETIC ACTION OF PHOSPHATASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,178,2,655-667,"Otto. Meyerhof, Harry. Green",en
+109,49MEY/OES,18134595.0,10.1016/S0021-9258(18)56800-9,,['THE ENZYMATIC EQUILIBRIA OF PHOSPHO(ENOL)PYRUVATE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,179,3,1371-1385,"Otto. Meyerhof, Peter. Oesper",en
+110,49SOR/DVO,,,,-,-,-,-,-,-,-,-,-,-
+111,50COR/VEL,,10.1016/0006-3002(50)90020-5,,-,-,-,-,-,-,-,-,-,-
+112,50FRI,15428423.0,10.1016/S0021-9258(19)50973-5,,['DESOXYRIBOSE-1-PHOSPHATE'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,184,2,449-459,Morris Friedkin,en
+113,50HES,,10.1016/0006-3002(50)90037-0,,-,-,-,-,-,-,-,-,-,-
+114,50KOR,,10.1016/S0021-9258(18)56513-3,,['REVERSIBLE ENZYMATIC SYNTHESIS OF DIPHOSPHOPYRIDINE NUCLEOTIDE AND INORGANIC PYROPHOSPHATE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,182,2,779-793,Arthur. Kornberg,en
+115,50OES/MEY,15419792.0,,,-,-,-,-,-,-,-,-,-,-
+116,50PAZ,,,,-,-,-,-,-,-,-,-,-,-
+117,50RAC,15443900.0,10.1016/S0021-9258(19)51151-6,,"[""CRYSTALLINE ALCOHOL DEHYDROGENASE FROM BAKERS' YEAST""]",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,184,1,313-319,E. Racker,en
+118,50SLE,14794671.0,10.1016/S0021-9258(18)56269-4,,['PHOSPHOMANNOSE ISOMERASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,186,2,753-761,Milton W. Slein,en
+119,51BLA,14858331.0,10.1042/bj0490257,,-,-,-,-,-,-,-,-,-,-
+120,51BLI,14830226.0,10.1016/0003-9861(51)90206-8,,['The equilibrium between vitamin A alcohol and aldehyde in the presence of alcohol dehydrogenase'],26.11.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,31,2,197-204,Alfred F. Bliss,en
+121,51FRU/JOH,14841149.0,10.1016/S0021-9258(18)56043-9,,['ELONGATION OF PEPTIDE CHAINS IN ENZYME-CATALYZED TRANSAMIDATION REACTIONS'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,190,1,39-53,"Joseph S. Fruton, Robert B. Johnston, Melvin. Fried",en
+122,51KOR,,,,-,-,-,-,-,-,-,-,-,-
+123,51ROW/KOR,14907738.0,10.1016/S0021-9258(18)50905-4,,['THE PHOSPHOROLYSIS OF NICOTINAMIDE RIBOSIDE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,193,2,497-507,"John W. Rowen, Arthur Kornberg",en
+124,51THE/BON,,10.3891/acta.chem.scand.05-1105,,-,-,-,-,-,-,-,-,-,-
+125,51WOO/GUN,14841188.0,10.1016/S0021-9258(18)56082-8,,['d-ALANINE FORMATION: A RACEMASE IN STREPTOCOCCUS FAECALIS'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,190,1,403-416,"W.A. Wood, I.C. Gunsalus",en
+126,52ASK,,,,-,-,-,-,-,-,-,-,-,-
+127,52BAU/GEM,14915545.0,10.1016/s0003-9861(52)80055-4,,['The heat produced by the enzymatic action of the sucrose-invertase and urea-urease systems'],7.7.2006,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,35,1,110-120,"C.R. Bauer, C.L. Gemmill",en
+128,52BUR,,10.1016/0006-3002(52)90020-6,,-,-,-,-,-,-,-,-,-,-
+129,52DOB/FRU,14938363.0,10.1016/S0021-9258(19)50883-3,,['THERMODYNAMICS OF HYDROLYSIS OF PEPTIDE BONDS'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,195,1,149-154,"Alan Dobry, Joseph S. Fruton, Julian M. Sturtevant",en
+130,52DOB/STU,14938362.0,10.1016/S0021-9258(19)50882-1,,['HEATS OF HYDROLYSIS OF AMIDE AND PEPTIDE BONDS'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,195,1,141-147,"Alan Dobry, Julian M. Sturtevant",en
+131,52EGG/HEM,13018181.0,10.1042/bj0520156,,-,-,-,-,-,-,-,-,-,-
+132,52FIT/DOU,12999827.0,10.1016/S0021-9258(18)44822-3,,['PHOSPHOROLYSIS OF MALTOSE BY ENZYME PREPARATIONS FROM NEISSERIA MENINGITIDIS'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,199,1,153-163,"Charlotte Fitting, Michael Doudoroff",en
+133,52KOR,,,,-,-,-,-,-,-,-,-,-,-
+134,52LEL/CAR,,,,-,-,-,-,-,-,-,-,-,-
+135,52MEY/SHA,12997210.0,10.1016/0003-9861(52)90109-4,,['Heat of hydrolysis of acetyl phosphate'],25.11.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,40,2,253-262,"Otto Meyerhof, Romas Shatas",en
+136,52NAR/WOO,14924668.0,10.1016/s0003-9861(52)80026-8,,['Evidence for a glutamic acid racemase in Lactobacillus arabinosus'],7.7.2006,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,35,2,462-463,"S.A. Narrod, W.A. Wood",en
+137,52NEI,12999850.0,10.1016/S0021-9258(18)44845-4,,['STUDIES ON LACTIC DEHYDROGENASE OF HEART'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,199,1,373-381,J.B. Neilands,en
+138,52OHL/SHA,14944266.0,10.1016/0003-9861(52)90426-8,,['Heat of hydrolysis of some phosphate compounds'],26.11.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,36,2,411-420,"Paul Ohlmeyer, Romas Shatas",en
+139,52STA,12980996.0,10.1016/S0021-9258(19)52387-0,,['THE NET ENZYMATIC SYNTHESIS OF ACETYL COENZYME A'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,196,2,535-546,E.R. Stadtman,en
+140,52STE/OCH,12999746.0,10.1016/S0021-9258(18)55585-X,,['ENZYMATIC SYNTHESIS OF CITRIC ACID'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,198,1,313-321,"Joseph R. Stern, Severo. Ochoa, Feodor. Lynen",en
+141,52STR/KOR,12981017.0,10.1016/S0021-9258(19)52408-5,,['GLUCOSE DEHYDROGENASE'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,196,2,769-784,"Harold J. Strecker, Seymour Korkes",en
+142,53BOC/ALB,,10.1021/ja01104a043,,-,-,-,-,-,-,-,-,-,-
+143,53BOD,13061507.0,10.1016/S0021-9258(18)66196-4,,['SERUM PHOSPHOHEXOSE ISOMERASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,202,2,829-840,Oscar Bodansky,en
+144,53BRI,,10.3891/acta.chem.scand.07-1081,,-,-,-,-,-,-,-,-,-,-
+145,53BRO,13117866.0,10.1016/S0021-9258(18)66092-2,,['ACTION OF PHOSPHOGLUCOMUTASE ON d-GLUCOSAMINE-6-PHOSPHATE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,204,2,877-889,David H. Brown,en
+146,53BUR/STA,13061511.0,10.1016/S0021-9258(18)66200-3,,['THE OXIDATION OF ACETALDEHYDE TO ACETYL COENZYME A'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,202,2,873-890,"Robert Main Burton, E.R. Stadtman",en
+147,53BUR/WIL,13058837.0,10.1042/bj0540086,,-,-,-,-,-,-,-,-,-,-
+148,53COH,13044776.0,10.1016/S0021-9258(18)71349-5,,['STUDIES ON d-RIBULOSE AND ITS ENZYMATIC CONVERSION TO d-ARABINOSE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,201,1,71-84,Seymour S. Cohen,en
+149,53GRE/BRO,13117926.0,10.1016/S0021-9258(19)77273-1,,['ADENOSINETRIPHOSPHATASE SYSTEMS OF MUSCLE'],7.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,205,1,493-501,"Irving Green, Joshua R.C. Brown, W.F.H.M. Mommaerts",en
+150,53HAR/KOR,13084629.0,10.1016/S0021-9258(19)52329-8,,['BIOSYNTHESIS OF DICARBOXYLIC ACIDS BY CARBON DIOXIDE FIXATION'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,203,2,595-604,"Isaac Harary, Saul R. Korey, Severo Ochoa",en
+151,53HOC/WAT,,10.1021/ja01109a516,,-,-,-,-,-,-,-,-,-,-
+152,53JON,13107745.0,,,-,-,-,-,-,-,-,-,-,-
+153,53KAP/COL,13117879.0,10.1016/S0021-9258(19)77226-3,,['PYRIDINE NUCLEOTIDE TRANSHYDROGENASE'],7.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,205,1,1-15,"Nathan O. Kaplan, Sidney P. Colowick, Elizabeth F. Neufeld",en
+154,53KRE,13058835.0,10.1042/bj0540078,,-,-,-,-,-,-,-,-,-,-
+155,53KRE2,13058836.0,10.1042/bj0540082,,-,-,-,-,-,-,-,-,-,-
+156,53LYN/OCH,,10.1016/0006-3002(53)90149-8,,['Enzymes of fatty acid metabolism'],10.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,12,1-2,299-314,"Feodor Lynen, Severo Ochoa",en
+157,53MAH/WAK,13084616.0,10.1016/S0021-9258(18)66153-8,,['STUDIES ON FATTY ACID OXIDATION'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,204,1,453-468,"H.R. Mahler, Salih J. Wakil, Robert M. Bock",en
+158,53MAS,13032036.0,10.1042/bj0530072,,-,-,-,-,-,-,-,-,-,-
+159,53MEY/SHA,,10.1016/0006-3002(53)90130-9,,['Heat of hydrolysis of trimetaphosphate'],10.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,12,1-2,121-127,"Otto Meyerhof, Romas Shatas, Ann Kaplan",en
+160,53MIT/LAM,13117877.0,10.1016/S0021-9258(18)66103-4,,['CONVERSION OF d-XYLOSE TO d-XYLULOSE IN EXTRACTS OF LACTOBACILLUS PENTOSUS'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,204,2,1011-1018,"S. Mitsuhashi, J.O. Lampen",en
+161,53NIS/BAR,13117873.0,10.1016/S0021-9258(18)66099-5,,['MECHANISMS IN ENZYMATIC TRANSAMINATION'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,204,2,957-969,"Alfred Nisonoff, Frederick W. Barnes, Theodore Enns",en
+162,53OLS/ANF,13061508.0,10.1016/S0021-9258(18)66197-6,,['KINETIC AND EQUILIBRIUM STUDIES ON CRYSTALLINE l-GLUTAMIC ACID DEHYDROGENASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,202,2,841-856,"James A. Olson, Christian B. Anfinsen",en
+163,53RAT/ANS,13084582.0,10.1016/S0021-9258(18)66119-8,,['BIOSYNTHESIS OF UREA'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,204,1,115-125,"S. Ratner, W. Parker Anslow, Barbara Petrack",en
+164,53SIE/POT,13034773.0,10.1016/S0021-9258(18)38451-5,,['The Adenylate Kinase of Rat Liver Mitochondria'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,200,1,187-196,"Philip Siekevitz, Van R. Potter",en
+165,53STE/COO,,10.1021/ja01102a540,,-,-,-,-,-,-,-,-,-,-
+166,53STR,13092953.0,10.1016/0003-9861(53)90176-3,,['Glutamic dehydrogenase'],7.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,46,1,128-140,Harold J. Strecker,en
+167,53STU,,10.1021/ja01104a527,,-,-,-,-,-,-,-,-,-,-
+168,53TAL/DOB,13129261.0,10.1016/S0021-9258(18)49226-5,,['PURIFICATION AND PROPERTIES OF A β-HYDROXYSTEROID DEHYDROGENASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,205,2,823-837,"Paul Talalay, Marie Mollomo Dobson",en
+169,54AXE/JAN,13192139.0,10.1016/S0021-9258(18)65513-9,,['PURIFICATION AND PROPERTIES OF PHOSPHORIBOISOMERASE FROM ALFALFA'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,209,2,847-855,"Bernard Axelrod, Rosie Jang",en
+170,54BER/JOK,13211603.0,10.1016/S0021-9258(18)65392-X,,['ENZYMATIC PHOSPHORYLATION OF NUCLEOSIDE DIPHOSPHATES'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,210,2,657-672,"Paul Berg, W.K. Joklik",en
+171,54BOW/KER,13139680.0,10.1016/0003-9861(54)90176-9,,['The kinetics of myokinase. I. Studies of the effects of salts and ph and of the state of equilibrium'],7.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,49,1,149-159,"William J. Bowen, Timothy D. Kerwin",en
+172,54CHA,13211661.0,10.1016/S0021-9258(18)71215-5,,['MECHANISM OF FORMATION OF ERYTHRULOSE-1-PHOSPHATE BY PHOSPHOKETOTETROSE ALDOLASE OF RAT LIVER'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,211,1,249-262,Frixos C. Charalampous,en
+173,54GIN,,,,-,-,-,-,-,-,-,-,-,-
+174,54GIN/STU,,10.1021/ja01637a015,,-,-,-,-,-,-,-,-,-,-
+175,54GOL,13174544.0,10.1016/S0021-9258(18)65653-4,,['STUDIES ON THE FATTY ACID OXIDIZING SYSTEM OF ANIMAL TISSUES'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,208,1,345-357,Dexter S. Goldman,en
+176,54GRE/MII,13130521.0,10.1016/S0021-9258(18)71290-8,,['STUDIES ON THE FATTY ACID OXIDIZING SYSTEM OF ANIMAL TISSUES'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,206,1,1-12,"D.E. Green, S. Mii, H.R. Mahler, Robert M. Bock",en
+177,54HAN/CRA,13174537.0,10.1016/S0021-9258(18)65646-7,,['LACTOSE METABOLISM'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,208,1,293-298,"R.G. Hansen, E.M. Craine, Patricia Gray",en
+178,54HEL,13143026.0,10.1016/S0021-9258(19)50835-3,,['THE ACETATE ACTIVATING ENZYME OF BEEF HEART'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,206,2,671-676,P. Hele,en
+179,54HOC/WAT,,10.1016/0003-9861(54)90313-6,,['Enzymatic isomerization of d-xylose to d-xylulose'],26.11.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,48,1,120-129,"R.M. Hochster, R.W. Watson",en
+180,54LEV/MEI,13192082.0,10.1016/S0021-9258(18)65554-1,,['REVERSIBILITY OF THE ENZYMATIC SYNTHESIS OF GLUTAMINE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,209,1,265-280,"Leon Levintow, Alton Meister",en
+181,54LIE/KOR,13163076.0,10.1016/S0021-9258(18)65708-4,,"['ENZYMATIC SYNTHESIS AND BREAKDOWN OF A PYRIMIDINE, OROTIC ACID']",5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,207,2,911-924,"Irving Lieberman, Arthur Kornberg",en
+182,54MAR/WIL,13159289.0,10.1016/0003-9861(54)90211-8,,['The alanine racemase of Brucella abortus'],7.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,49,2,424-433,"A.G. Marr, P.W. Wilson",en
+183,54MIT/DAV,,10.1016/0006-3002(54)90093-1,,['Aromatic biosynthesis'],10.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,15,1,54-61,"Susumu Mituhashi, Bernard D. Davis",en
+184,54NOD/KUB,,10.1016/S0021-9258(18)65434-1,,['ADENOSINETRIPHOSPHATE-CREATINE TRANSPHOSPHORYLASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,210,1,83-95,"Lafayette Noda, Stephen A. Kuby, Henry A. Lardy",en
+185,54ROS/GRU,13221579.0,10.1016/S0021-9258(18)71161-7,,['ENZYMATIC PHOSPHORYLATION OF ACETATE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,211,2,737-756,"Irwin A. Rose, Marianne Grunberg-Manago, Saul R. Korey, Severo Ochoa",en
+186,54SIS/STA,13211620.0,10.1016/S0021-9258(18)65409-2,,['THE MECHANISM OF FORMATION OF β-KETOADIPIC ACID BY BACTERIA'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,210,2,821-836,"W.R. Sistrom, R.Y. Stanier",en
+187,54STA,,,,-,-,-,-,-,-,-,-,-,-
+188,54STR/HAR,13211662.0,10.1016/S0021-9258(18)71216-7,,['BACTERIAL BUTYLENE GLYCOL DEHYDROGENASE AND DIACETYL REDUCTASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,211,1,263-270,"Harold J. Strecker, Isaac Harary",en
+189,54UTT/KUR,13163068.0,10.1016/S0021-9258(18)65700-X,,['MECHANISM OF ACTION OF OXALACETIC CARBOXYLASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,207,2,821-841,"M.F. Utter, K. Kurahashi",en
+190,54WAK/GRE,13163047.0,10.1016/S0021-9258(18)65679-0,,['STUDIES ON THE FATTY ACID OXIDIZING SYSTEM OF ANIMAL TISSUES'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,207,2,631-638,"Salih J. Wakil, D.E. Green, S. Mii, H.R. Mahler",en
+191,54WIL/BAN,13159356.0,10.1016/0003-9861(54)90072-7,,['The ketose reductase of rat liver and accessory sexual organs'],10.2.2005,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,50,2,513-515,"H.G. Williams-Ashman, J. Banks",en
+192,55BLA/WRI,14353903.0,10.1016/S0021-9258(18)71041-7,,['β-ASPARTOKINASE AND β-ASPARTYL PHOSPHATE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,213,1,27-38,"Simon Black, Nancy G. Wright",en
+193,55BLA/WRI2,14353904.0,10.1016/S0021-9258(18)71042-9,,['ASPARTIC β-SEMIALDEHYDE DEHYDROGENASE AND ASPARTIC β-SEMIALDEHYDE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,213,1,39-50,"Simon Black, Nancy G. Wright",en
+194,55BLA/WRI3,14353905.0,10.1016/S0021-9258(18)71043-0,,['HOMOSERINE DEHYDROGENASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,213,1,51-60,"Simon Black, Nancy G. Wright",en
+195,55BUC,,10.1016/0076-6879(55)01068-9,,-,-,-,-,-,-,-,-,-,-
+196,55BUR,,10.1016/0076-6879(55)01063-X,,-,-,-,-,-,-,-,-,-,-
+197,55CAR/COH,,10.1021/ja01607a095,,-,-,-,-,-,-,-,-,-,-
+198,55CAR/LEL,14367373.0,10.1016/S0021-9258(18)70953-8,,['THE BIOSYNTHESIS OF SUCROSE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,214,1,149-155,"C.E. Cardini, Luis F. Leloir, J. Chiriboga",en
+199,55DAV/GIL,,10.1016/S0076-6879(55)02203-9,,-,-,-,-,-,-,-,-,-,-
+200,55DEC,,,,-,-,-,-,-,-,-,-,-,-
+201,55DIC/WIL,,10.1038/176400a0,,['Transformation of Pentose Phosphates by Enzymes of Animal Origin'],30.5.2006,Springer Science and Business Media LLC,http://www.springer.com/tdm,journal-article,176,4478,400-401,"FRANK DICKENS, D. H. WILLTAMSON",en
+202,55GLA/BRO,13252007.0,10.1016/S0021-9258(19)52284-0,,['PURIFICATION AND PROPERTIES OF d-GLUCOSE-6-PHOSPHATE DEHYDROGENASE'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,216,1,67-79,"Luis Glaser, David H. Brown",en
+203,55GRI/WAL,,10.1016/0006-3002(55)90122-0,,-,-,-,-,-,-,-,-,-,-
+204,55HOR/SMY,14353883.0,10.1016/S0021-9258(18)71020-X,,['PURIFICATION AND PROPERTIES OF YEAST TRANSALDOLASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,212,2,811-825,"B.L. Horecker, P.Z. Smyrniotis",en
+205,55KAT,,10.1016/0006-3002(55)90353-X,,-,-,-,-,-,-,-,-,-,-
+206,55KAU/ALI,13252014.0,10.1016/S0021-9258(19)52291-8,,['PURIFICATION AND PROPERTIES OF THE PHOSPHORYLATING ENZYME FROM SPINACH'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,216,1,141-152,"Seymour Kaufman, Spyridon G.A. Alivisatos",en
+207,55KIT/BEN,,10.1515/znb-1955-0704,,['Wärmetönung der Adenosintriphosphorsäure-Spaltung'],27.2.2015,Walter de Gruyter GmbH,http://creativecommons.org/licenses/by-nc-nd/3.0/,journal-article,10,7,375-382,"C. Kitzinger, T. Benzinger",en
+208,55LEH/SIC,,10.1016/0006-3002(55)90368-1,,-,-,-,-,-,-,-,-,-,-
+209,55LIE/KOR,14392174.0,10.1016/S0021-9258(18)66048-X,,"[""ENZYMATIC SYNTHESIS OF PYRIMIDINE NUCLEOTIDES. OROTIDINE-5'-PHOSPHATE AND URIDINE-5'-PHOSPHATE""]",5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,215,1,403-415,"Irving Lieberman, Arthur Kornberg, Ernest S. Simms",en
+210,55LIE/KOR2,14392176.0,10.1016/S0021-9258(18)66050-8,,['ENZYMATIC SYNTHESIS OF NUCLEOSIDE DIPHOSPHATES AND TRIPHOSPHATES'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,215,1,429-440,"Irving Lieberman, Arthur Kornberg, Ernest S. Simms",en
+211,55LYN/WIE,,10.1016/0076-6879(55)01099-9,,-,-,-,-,-,-,-,-,-,-
+212,55MUN,,10.3891/acta.chem.scand.09-1523,,-,-,-,-,-,-,-,-,-,-
+213,55POD/STU,13271421.0,10.1016/S0021-9258(18)65925-3,,['THE ENTHALPY CHANGE ON ADENOSINE TRIPHOSPHATE HYDROLYSIS. I'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,217,2,603-606,"Richard J. Podolsky, Julian M. Sturtevant",en
+214,55SLE,,10.1021/ja01611a074,,-,-,-,-,-,-,-,-,-,-
+215,55STA,,10.1016/0076-6879(55)01103-8,,-,-,-,-,-,-,-,-,-,-
+216,55STA/BUR,,10.1016/0076-6879(55)01089-6,,-,-,-,-,-,-,-,-,-,-
+217,55STU,,10.1021/ja01607a001,,-,-,-,-,-,-,-,-,-,-
+218,55STU2,,10.1021/ja01611a026,,-,-,-,-,-,-,-,-,-,-
+219,55THO/GOM,14367287.0,10.1128/jb.69.3.357-362.1955,,['TRANSAMINATION OF\n d\n -AMINO ACIDS BY BACILLUS SUBTILIS'],3.1.2020,American Society for Microbiology,https://journals.asm.org/non-commercial-tdm-license,journal-article,69,3,357-362,"Curtis B. Thorne, Carmen G. Gómez, Riley D. Housewright",en
+220,55VAR/WEB,16654798.0,10.1104/pp.30.5.393,,['Studies on the Enzymatic Synthesis of Glutamine'],13.12.2008,Oxford University Press (OUP),http://aspb.org/publications/aspb-journals/open-articles,journal-article,30,5,393-402,"J. E. Varner, George C. Webster",en
+221,55WIL/MCI,13271408.0,10.1016/S0021-9258(19)57195-2,,['PREPARATION AND PARTIAL PURIFICATION OF THE ASPARTASE OF BACTERIUM CADAVERIS'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,217,1,467-477,"Virginia R. Williams, Russell T. McIntyre",en
+222,55WOL/KAP,,10.1016/0076-6879(55)01050-1,,-,-,-,-,-,-,-,-,-,-
+223,55YAN/GIL,14367339.0,10.1016/S0021-9258(18)98210-4,,['AROMATIC BIOSYNTHESIS'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,213,2,787-795,"Haim Yaniv, Charles Gilvarg",en
+224,55ZEL,13271335.0,10.1016/S0021-9258(19)81413-8,,['THE ISOLATION AND ACTION OF CRYSTALLINE GLYOXYLIC ACID REDUCTASE FROM TOBACCO LEAVES'],7.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,216,2,553-575,Israel Zelitch,en
+225,56ALE/GRE,13331936.0,10.1016/S0021-9258(18)65303-7,,['STUDIES ON THE PURIFICATION AND PROPERTIES OF THE SERINE-FORMING ENZYME SYSTEM'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,220,2,775-785,"Nicholas Alexander, David M. Greenberg",en
+226,56AME/HOR,13319331.0,10.1016/S0021-9258(18)65337-2,,['THE BIOSYNTHESIS OF HISTIDINE: IMIDAZOLEACETOL PHOSPHATE TRANSAMINASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,220,1,113-128,"Bruce N. Ames, B.L. Horecker",en
+227,56BEN/HEM,16589970.0,10.1073/pnas.42.12.896,,-,-,-,-,-,-,-,-,-,-
+228,56BOW/KER,13363434.0,10.1016/0003-9861(56)90270-3,,"['The kinetics of myokinase. II. Studies of heat denaturation, the effects of salts and the state of equilibrium']",10.2.2005,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,64,2,278-284,"William J. Bowen, Timothy D. Kerwin",en
+229,56CAR/COH,13366975.0,10.1016/S0021-9258(19)50767-0,,['THE PREPARATION AND PROPERTIES OF ADENYLOSUCCINASE AND ADENYLOSUCCINIC ACID'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,222,1,17-30,"Charles E. Carter, Leonard H. Cohen",en
+230,56COW/PIZ,13385236.0,10.1016/S0021-9258(18)65087-2,,['PURIFICATION AND SOME PROPERTIES OF PHOSPHORYLGLYCERIC ACID MUTASE FROM RABBIT SKELETAL MUSCLE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,223,2,885-895,"Robert W. Cowgill, Lewis I. Pizer",en
+231,56DIC/WIL,13373810.0,10.1042/bj0640567,,-,-,-,-,-,-,-,-,-,-
+232,56ENG,,,,-,-,-,-,-,-,-,-,-,-
+233,56FEU/WOL,13354402.0,,,-,-,-,-,-,-,-,-,-,-
+234,56FOR/GUT,,10.1021/ja01588a024,,-,-,-,-,-,-,-,-,-,-
+235,56GRE/COH,13319278.0,10.1016/S0021-9258(18)65716-3,,['ENZYMATIC CONVERSION OF l-FUCOSE TO l-FUCULOSE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,219,2,557-568,"Maurice Green, Seymour S. Cohen",en
+236,56HAK/GLA,13345810.0,10.1016/S0021-9258(18)65240-8,,['LACTIC DEHYDROGENASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,221,1,191-209,"Maire T. Hakala, Andrew J. Glaid, George W. Schwert",en
+237,56HAU,,10.1021/ja01601a032,,-,-,-,-,-,-,-,-,-,-
+238,56HUB,,10.1085/jgp.39.6.935,,-,-,-,-,-,-,-,-,-,-
+239,56HUR/HOR,13385247.0,10.1016/S0021-9258(18)65098-7,,['THE PURIFICATION OF PHOSPHOKETOPENTOEPIMERASE FROM LACTOBACILLUS PENTOSUS AND THE PREPARATION OF XYLULOSE 5-PHOSPHATE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,223,2,993-1008,"Jerard Hurwitz, B.L. Horecker",en
+240,56KAP/CIO,13357478.0,10.1016/S0021-9258(18)65197-X,,['REACTION OF PYRIDINE NUCLEOTIDE ANALOGUES WITH DEHYDROGENASES'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,221,2,833-844,"Nathan O. Kaplan, Margaret M. Ciotti, Francis E. Stolzenbach",en
+241,56KIT/HOR,,,,-,-,-,-,-,-,-,-,-,-
+242,56LAR/JAC,13292912.0,10.1016/0003-9861(56)90437-4,,['Inositol dehydrogenase from Aerobacter aerogenes'],26.11.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,60,2,352-363,"J. Larner, W.T. Jackson, D.J. Graves, J.R. Stamer",en
+243,56LEL/CAR,,10.1016/0006-3002(56)90259-1,,-,-,-,-,-,-,-,-,-,-
+244,56PAL/DOU,13278359.0,10.1016/S0021-9258(18)65915-0,,['MANNOSE ISOMERASE OF PSEUDOMONAS SACCHAROPHILA'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,218,1,535-548,"Norberto J. Palleroni, Michael Doudoroff",en
+245,56POD/MOR,13295245.0,10.1016/S0021-9258(18)65857-0,,['THE ENTHALPY CHANGE OF ADENOSINE TRIPHOSPHATE HYDROLYSIS'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,218,2,945-959,"Richard J. Podolsky, Manuel F. Morales",en
+246,56RAB/PRI,,10.1021/ja01597a094,,-,-,-,-,-,-,-,-,-,-
+247,56RAM/GIR,13314642.0,10.1016/0003-9861(56)90091-1,,"['Phosphoglucose isomerase11Slein (6) has pointed out that the two isomerases which convert G-6-P and mannose 6-phosphate (M-6-P) into F-6-P, may now be more descriptively called phosphoglucose isomerase and phosphomannose isomerase, respectively, since it is now known that F-6-P is the product of M-6-P isomerization also. We propose to adopt this nomenclature. of green gram (Phaseolus radiatus)']",25.11.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,62,1,91-96,"T. Ramasarma, K.V. Giri",en
+248,56RAT/ROC,13355454.0,10.1016/0003-9861(56)90044-3,,['Biosynthesis of guanidinoacetic acid. I. Purification and properties of transamidinase'],8.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,63,2,277-295,"S. Ratner, Olga Rochovansky",en
+249,56REI,13319297.0,10.1016/S0021-9258(18)65735-7,,['PHOSPHOACETYLGLUCOSAMINE MUTASE OF NEUROSPORA'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,219,2,753-767,José L. Reissig,en
+250,56SMI/STA,,10.1016/0006-3002(56)90493-0,,-,-,-,-,-,-,-,-,-,-
+251,56STE,13345796.0,10.1016/S0021-9258(18)65226-3,,['OPTICAL PROPERTIES OF ACETOACETYL-S-COENZYME A AND ITS METAL CHELATES'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,221,1,33-44,Joseph R. Stern,en
+252,56STE/COO,13345795.0,10.1016/S0021-9258(18)65225-1,,['ENZYMES OF FATTY ACID METABOLISM'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,221,1,15-31,"Joseph R. Stern, Minor J. Coon, Alice del Campillo, Morton C. Schneider",en
+253,56STE/DEL,13295248.0,10.1016/S0021-9258(18)65860-0,,['ENZYMES OF FATTY ACID METABOLISM'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,218,2,985-1002,"Joseph R. Stern, Alice del Campillo",en
+254,56STU/HOR,13295228.0,10.1016/S0021-9258(18)65840-5,,['THE RÔLE OF XYLULOSE 5-PHOSPHATE IN XYLOSE METABOLISM OF LACTOBACILLUS PENTOSUS'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,218,2,753-768,"P.K. Stumpf, B.L. Horecker",en
+255,56TAL/MAR,13295222.0,10.1016/S0021-9258(18)65834-X,,"['SPECIFICITY, KINETICS, AND INHIBITION OF α- AND β-HYDROXYSTEROID DEHYDROGENASES']",5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,218,2,675-691,"Paul Talalay, Philip I. Marcus",en
+256,56TOM,13278351.0,10.1016/S0021-9258(18)65907-1,,['A MAMMALIAN 3α-HYDROXYSTEROID DEHYDROGENASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,218,1,437-447,Gordon M. Tomkins,en
+257,56WOL/KAP,13295236.0,10.1016/S0021-9258(18)65848-X,,['d-MANNITOL 1-PHOSPHATE DEHYDROGENASE FROM ESCHERICHIA COLI'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,218,2,849-869,"John B. Wolfe, Nathan O. Kaplan",en
+258,57ASH/HIC,13428737.0,10.1016/S0021-9258(18)64805-7,,['ENZYMATIC FORMATION OF XYLULOSE 5-PHOSPHATE FROM RIBOSE 5-PHOSPHATE IN SPLEEN'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,226,1,65-76,"Gilbert Ashwell, Jean Hickman",en
+259,57BUR/HOR,,10.1016/0006-3002(57)90272-X,,-,-,-,-,-,-,-,-,-,-
+260,57CAL,13488919.0,10.1042/bj0670651,,-,-,-,-,-,-,-,-,-,-
+261,57DOU/CON,,,,-,-,-,-,-,-,-,-,-,-
+262,57DUR/STU,,10.1016/0006-3002(57)90006-9,,['The synthesis of methionine by enzymic transmethylation II. Enthalpy change in the methyl-transfer from dimethylacetothetin'],10.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,26,2,282-286,"J. Durell, J.M. Sturtevant",en
+263,57FLA/ERW,13475309.0,10.1016/S0021-9258(18)70703-5,,['BIOSYNTHESIS OF THE PURINES'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,228,1,201-213,"Joel G. Flaks, Mary Jane Erwin, John M. Buchanan",en
+264,57GRE/LIP,13502367.0,10.1016/S0021-9258(19)63710-5,,"[""THE TRANSFER OF SULFATE AMONG PHENOLIC COMPOUNDS WITH 3',5'-DIPHOSPHOADENOSINE AS COENZYME""]",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,229,2,1081-1090,"John D. Gregory, Fritz Lipmann",en
+265,57HOH,13426146.0,,,-,-,-,-,-,-,-,-,-,-
+266,57HOL/HOL,13522707.0,,,-,-,-,-,-,-,-,-,-,-
+267,57HOL/TOU,13416220.0,10.1016/S0021-9258(18)64912-9,,['THE l-XYLULOSE-XYLITOL ENZYME AND OTHER POLYOL DEHYDROGENASES OF GUINEA PIG LIVER MITOCHONDRIA'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,225,1,87-102,"Siegfried Hollmann, Oscar Touster",en
+268,57KAR/GRE,13449064.0,10.1016/S0021-9258(18)70806-5,,['STUDIES ON THE PROPERTIES OF THREONINE ALDOLASES'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,227,1,191-205,"Marvin A. Karasek, David M. Greenberg",en
+269,57MAX,13491567.0,10.1016/S0021-9258(18)70602-9,,['THE ENZYMIC INTERCONVERSION OF URIDINE DIPHOSPHOGALACTOSE AND URIDINE DIPHOSPHOGLUCOSE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,229,1,139-151,Elizabeth S. Maxwell,en
+270,57REI,,10.3891/acta.chem.scand.11-0523,,-,-,-,-,-,-,-,-,-,-
+271,57ROB/BOY,13398392.0,10.1016/S0021-9258(18)65015-X,,['DETERMINATION OF THE EQUILIBRIUM OF THE HEXOKINASE REACTION AND THE FREE ENERGY OF HYDROLYSIS OF ADENOSINE TRIPHOSPHATE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,224,1,121-135,"E.A. Robbins, P.D. Boyer",en
+272,57ROB/COO,13416257.0,10.1016/S0021-9258(18)64948-8,,['THE PURIFICATION AND PROPERTIES OF β-HYDROXYISOBUTYRIC DEHYDROGENASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,225,1,511-521,"William G. Robinson, Minor J. Coon",en
+273,57ROD/TOW,13475367.0,10.1016/S0021-9258(18)70667-4,,['The Kinetic Properties Of Yeast And Muscle Phosphoglyceric Acid Mutase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,228,2,875-890,"Victor W. Rodwell, Jack C. Towne, Santiago Grisolia",en
+274,57SAN/SEA,,10.1016/0006-3002(57)90179-8,,-,-,-,-,-,-,-,-,-,-
+275,57SMI/GUN,13491582.0,10.1016/S0021-9258(18)70617-0,,['ISOCITRITASE: ENZYME PROPERTIES AND REACTION EQUILIBRIUM'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,229,1,305-319,"Roberts A. Smith, I.C. Gunsalus",en
+276,57STE,,10.1016/0006-3002(57)90040-9,,['Crystalline β-hydroxybutyryl dehydrogenase from pig heart'],10.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,26,2,448-449,Joseph R. Stern,en
+277,57TAL,,,,-,-,-,-,-,-,-,-,-,-
+278,57VLA/VLA,13499474.0,,,-,-,-,-,-,-,-,-,-,-
+279,57VLA/VLA2,13451618.0,10.1038/1791350a0,,['The Free Energy of Hydrolysis of Adenosine Triphosphoric Acid'],30.5.2006,Springer Science and Business Media LLC,http://www.springer.com/tdm,journal-article,179,4574,1350-1351,"G. E. VLADIMIROV, V. G. VLASSOVA, A. Y. KOLOTILOVA, S. N. LYZLOVA, N. S. PANTELEYEVA",en
+280,57WOL/BAL,,10.1016/S0021-9258(18)70816-8,,['STUDIES ON THE ENZYME ENOLASE'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,227,1,301-312,"Finn Wold, Clinton E. Ballou",en
+281,58BAC,,10.3891/acta.chem.scand.12-1279,,-,-,-,-,-,-,-,-,-,-
+282,58BRU/NOL,13596391.0,,,-,-,-,-,-,-,-,-,-,-
+283,58BUR/HOR,13539036.0,10.1016/S0021-9258(18)70466-3,,['PENTOSE FERMENTATION BY LACTOBACILLUS PLANTARUM'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,231,2,1053-1064,"D.P. Burma, B.L. Horecker",en
+284,58CAB/LEL,13538966.0,10.1016/S0021-9258(19)77303-7,,['THE BIOSYNTHESIS OF TREHALOSE PHOSPHATE'],7.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,231,1,259-275,"E. Cabib, Luis F. Leloir",en
+285,58FRO,,10.1016/0006-3002(58)90182-3,,['On the equilibrium and mechanism of adenylosuccinic acid synthesis'],10.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,29,2,255-262,Herbert J. Fromm,en
+286,58FRO2,13598730.0,10.1016/S0021-9258(19)77337-2,,['Ribitol Dehydrogenase'],7.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,233,5,1049-1052,Herbert J. Fromm,en
+287,58HEA/HOR,13539034.0,10.1016/S0021-9258(18)70464-X,,['PENTOSE FERMENTATION BY LACTOBACILLUS PLANTARUM'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,231,2,1031-1037,"E.C. Heath, B.L. Horecker, P.Z. Smyrniotis, Yasuyuki Takagi",en
+288,58LAN/ENG,13575417.0,10.1016/S0021-9258(18)64708-8,,['Human Placental Estradiol-17β Dehydrogenase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,233,3,583-588,"Lorna J. Langer, Lewis L. Engel",en
+289,58MAL/OCH,13610869.0,10.1016/S0021-9258(18)49368-4,,['Enzymatic Phosphorylation of Deoxycytidylic Acid'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,233,6,1538-1543,"Frank Maley, Severo Ochoa",en
+290,58MCQ,,,appears in part 2,-,-,-,-,-,-,-,-,-,-
+291,58NOL/BRU,13596394.0,,,-,-,-,-,-,-,-,-,-,-
+292,58ROB/LIP,13575437.0,10.1016/S0021-9258(18)64728-3,,['Enzymatic Synthesis of Adenosine-5′-Phosphosulfate'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,233,3,686-690,"Phillips W. Robbins, Fritz Lipmann",en
+293,58TAB/SRE,13534662.0,10.1016/0003-9861(58)90003-1,,"['The oxidative pentose phosphate cycle. III. The interconversion of ribose 5-phosphate, ribulose 5-phosphate and xylulose 5-phosphate']",25.11.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,74,2,315-325,"M. Tabachnick, P.A. Srere, J. Cooper, E. Racker",en
+294,58TUR/TUR,13560389.0,10.1042/bj0690448,,-,-,-,-,-,-,-,-,-,-
+295,58WIL/BAN,13587526.0,10.1016/S0021-9258(18)64689-7,,"['Enzymatic Reactions Involving Sulfate, Sulfite, Selenate, and Molybdate']",5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,233,4,975-981,"Lloyd G. Wilson, Robert S. Bandurski",en
+296,58WOL/SIM,13549442.0,10.1016/S0021-9258(18)70419-5,,['DEGRADATION OF l-ARABINOSE BY AEROBACTER AEROGENES'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,232,1,559-575,"M.J. Wolin, F.J. Simpson, W.A. Wood",en
+297,58YOU/PAC,13534693.0,10.1016/0003-9861(58)90403-x,,['Some physical and chemical properties of crystalline α-glycerophosphate dehydrogenase'],7.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,75,1,125-141,"Ho Lee Young, Nello Pace",en
+298,59ALE,,,,-,-,-,-,-,-,-,-,-,-
+299,59ATK/JOH,,10.1038/1841925a0,,['Equilibrium Constant of the Galactokinase Reaction and Free Energy of Hydrolysis of Adenosine Triphosphate'],30.5.2006,Springer Science and Business Media LLC,http://www.springer.com/tdm,journal-article,184,4703,1925-1927,"M. R. ATKINSON, ELEANOR JCHNSON, R. K. MORTON",en
+300,59BAR/SMY,13630903.0,10.1016/S0021-9258(18)70297-4,,['The Purification and Properties of β-Methylaspartase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,2,320-328,"H.A. Barker, R.D. Smyth, R. Marilyn Wilson, H. Weissbach",en
+301,59BEN/KIT,13628584.0,10.1042/bj0710400,,-,-,-,-,-,-,-,-,-,-
+302,59BON/PON,,10.1016/0006-291X(59)90066-X,,['The formation and cleavage of fructose catalyzed by transaldolase'],3.11.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,1,2,79-82,"A. Bonsignore, S. Pontremoli, E. Grazi, M. Mangiarotti",en
+303,59CAL/WEB,13806976.0,10.1042/bj0730473,,-,-,-,-,-,-,-,-,-,-
+304,59CHI/SUG,,10.1080/03758397.1959.10857560,,-,-,-,-,-,-,-,-,-,-
+305,59DEL/DEF,,10.1016/0006-3002(59)90495-0,,['2-ketogluconreductase in micro-organisms'],10.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,33,1,47-54,"J. De Ley, J. Defloor",en
+306,59DEN/ROB,13672942.0,10.1016/S0021-9258(18)69904-1,,['Enzymatic Conversion of β-Hydroxypropionate to Malonic Semialdehyde'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,7,1666-1671,"Halina Den, William G. Robinson, Minor J. Coon",en
+307,59FRI,13825045.0,10.1016/S0021-9258(18)69689-9,,['Glutamic Dehydrogenase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,11,2891-2896,Carl Frieden,en
+308,59GOL,,10.1016/0006-3002(59)90555-4,,-,-,-,-,-,-,-,-,-,-
+309,59HAB/CAN,13641268.0,10.1016/S0021-9258(18)70253-6,,['The Enzymatic Synthesis of S-Adenosyl-l-homocysteine from Adenosine and Homocysteine'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,3,603-608,"G. de la Haba, G.L. Cantoni",en
+310,59HOL,14402710.0,10.1515/bchm2.1959.317.1.193,,-,-,-,-,-,-,-,-,-,-
+311,59ITO/GRI,13630886.0,10.1016/S0021-9258(18)70280-9,,"['Phosphoglyceric Acid Mutase Activity without Added 2,3-Diphosphoglycerate in Preparations Purified from Wheat Germ']",5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,2,242-245,"N. Ito, Santiago Grisolia",en
+312,59KIR/TUR,14409347.0,10.1042/bj0720716,,-,-,-,-,-,-,-,-,-,-
+313,59KIT/HEM,13628583.0,10.1042/bj0710395,,-,-,-,-,-,-,-,-,-,-
+314,59KRI,13630884.0,10.1016/S0021-9258(18)70278-0,,['Phosphorylation of Pyruvate by the Pyruvate Kinase Reaction and Reversal of Glycolysis in a Reconstructed System'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,2,232-236,I. Krimsky,en
+315,59MCC/NAJ,,10.1016/S0021-9258(18)69716-9,,['The Purification and Mechanism of Action of Yeast Phosphoglucomutase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,11,3017-3021,"Ernest E. McCoy, Victor A. Najjar",en
+316,59MCQ/UTT,13673030.0,10.1016/S0021-9258(18)69883-7,,['Equilibrium and Kinetic Studies of the Pyruvic Kinase Reaction'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,8,2151-2157,"John T. McQuate, Merton F. Utter",en
+317,59MER/TOM,,10.1016/S0021-9258(18)69780-7,,['Reversible Oxidation of Cyclic Secondary Alcohols by Liver Alcohol Dehydrogenase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,10,2778-2782,"A. Donald Merritt, Gordon M. Tomkins",en
+318,59MIL/LUK,13672968.0,10.1016/S0021-9258(18)69930-2,,['Biosynthesis of the Purines'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,7,1806-1811,"Richard W. Miller, Lewis N. Lukens, John M. Buchanan",en
+319,59NOR/FRO,14427582.0,10.1016/S0021-9258(18)69732-7,,['Ribitol Dehydrogenase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,10,2523-2531,"Robert C. Nordlie, Herbert J. Fromm",en
+320,59SAN/LAN,13610916.0,10.1016/S0021-9258(18)70359-1,,['α-Ketoglutaric Dehydrogenase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,1,178-182,"D.R. Sanadi, Martha Langley, Robert L. Searls",en
+321,59SCO/JAK,13654294.0,10.1016/S0021-9258(18)70206-8,,['Soluble γ-Aminobutyric-Glutamic Transaminase from Pseudomonas fluorescens'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,4,932-936,"Edward M. Scott, William B. Jakoby",en
+322,59SHO/PRI,13664648.0,10.1128/jb.77.6.695-700.1959,,['d\n -SORBITOL-6-PHOSPHATE DEHYDROGENASE FROM\n LACTOBACILLUS CASEI'],3.1.2020,American Society for Microbiology,https://journals.asm.org/non-commercial-tdm-license,journal-article,77,6,695-700,"Thomas E. Shockley, Harold S. Pride",en
+323,59STR/SMI,13672971.0,10.1016/S0021-9258(18)69933-8,,['Uridine Diphosphoacetylglucosamine Pyrophosphorylase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,7,1822-1827,"Jack L. Strominger, Mildred S. Smith",en
+324,59TAB/WYN,13672973.0,10.1016/S0021-9258(18)69935-1,,"['The Enzymatic Formation of Formiminotetrahydrofolic Acid, 5,10-Methenyltetrahydrofolic Acid, and 10-Formyltetrahydrofolic Acid in the Metabolism of Formiminoglutamic Acid']",5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,7,1830-1846,"Herbert Tabor, Lillian Wyngarden",en
+325,59TAL/LEV,,,,-,-,-,-,-,-,-,-,-,-
+326,59VAG/EAR,13641247.0,10.1016/S0021-9258(18)70232-9,,['Propionic Acid Metabolism'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,234,3,490-497,"P. Roy Vagelos, Joan M. Earl, E.R. Stadtman",en
+327,60AGO/ARA,13681649.0,,,-,-,-,-,-,-,-,-,-,-
+328,60ASH/WAH,13794771.0,10.1016/S0021-9258(19)76840-9,,['Uronic Acid Metabolism in Bacteria'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,235,6,1559-1565,"Gilbert Ashwell, Albert J. Wahba, Jean Hickman",en
+329,60BLA,13801272.0,10.1042/bj0740071,,-,-,-,-,-,-,-,-,-,-
+330,60COM/ROS,13811398.0,10.1016/S0021-9258(19)76908-7,,['The Sialic Acids'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,235,9,2529-2537,"Donald G. Comb, Saul Roseman",en
+331,60FEI/NEU,13821949.0,10.1016/S0021-9258(18)69449-9,,['The 4-Epimerization and Decarboxylation of Uridine Diphosphate d-Glucuronic Acid by Extracts from Phaseolus aureus Seedlings'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,235,4,910-913,"David S. Feingold, Elizabeth F. Neufeld, W.Z. Hassid",en
+332,60GEL/STU,,10.1021/ja01491a053,,-,-,-,-,-,-,-,-,-,-
+333,60GUP/ROB,13830319.0,10.1016/S0021-9258(19)76849-5,,['The Enzymatic Conversion of Lactaldehyde to Propanediol'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,235,6,1609-1612,"Naba K. Gupta, William G. Robinson",en
+334,60ICH/FUR,,10.1093/oxfordjournals.jbchem.a127169,,-,-,-,-,-,-,-,-,-,-
+335,60ISH,,,,-,-,-,-,-,-,-,-,-,-
+336,60JON/LIP,16590733.0,10.1073/pnas.46.9.1194,,-,-,-,-,-,-,-,-,-,-
+337,60KAH/LOW,14408402.0,10.1016/S0021-9258(18)64594-6,,['The Kinetics of Phosphoglucoisomerase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,235,8,2178-2184,"Shirley E. Kahana, Oliver H. Lowry, Demoy W. Schulz, Janet V. Passonneau, Elizabeth J. Crawford",en
+338,60KAY/OSB,14404999.0,10.1016/S0021-9258(18)69609-7,,['The Enzymatic Conversion of N5-Formyl Tetrahydrofolic Acid (Folinic Acid) to N10-Formyl Tetrahydrofolic Acid'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,235,1,195-201,"L.D. Kay, M.J. Osborn, Y. Hatefi, F.M. Huennekens",en
+339,60KUR/SUG,14412847.0,10.1016/S0021-9258(18)69456-6,,['Purification and Properties of Galactose 1-Phosphate Uridyl Transferase from Escherichia coli'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,235,4,940-946,"K. Kurahashi, Akie Sugimura",en
+340,60LEA/GLA,13759914.0,10.1016/S0021-9258(20)81338-6,,['Incorporation of Amino Acids into Ribonucleic Acid'],7.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,235,11,3209-3212,"John Leahy, Edward Glassman, Richard S. Schweet",en
+341,60MAX/ROB,,10.1016/S0021-9258(18)69520-1,,"['Purification of Uridine Diphosphate Galactose-4-epimerase from Yeast, and the Identification of Protein-bound Diphosphopyridine Nucleotide']",5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,235,2,308-312,"Elizabeth S. Maxwell, Huguette de Robichon-Szulmajster",en
+342,60MEN,13769376.0,10.1016/S0021-9258(18)64469-2,,['Sucrose Phosphate Synthesis in Wheat Germ and Green Leaves'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,235,12,3347-3352,Joseph Mendicino,en
+343,60NIR/JAK,14427301.0,10.1016/S0021-9258(18)69459-1,,['Enzymatic Utilization of γ-Hydroxybutyric Acid'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,235,4,954-960,"Marshall W. Nirenberg, William B. Jakoby",en
+344,60OCO/HAL,13730045.0,10.1016/0003-9861(60)90503-8,,['Intermediate metabolism of aerobic spores. V. The purification and properties of l-alanine dehydrogenase'],25.11.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,91,2,290-299,"R.J. O'Connor, H.O. Halvorson",en
+345,60PIE/WIA,,10.1016/0006-3002(60)90506-0,,['Propriétés de la l(+)-alanine-déshydrogénase'],10.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,37,3,490-502,"A. Piérard, J.M. Wiame",fr
+346,60PRI/HOR,14434864.0,10.1016/S0021-9258(18)69401-3,,['Deoxyribose Aldolase from Lactobacillus plantarum'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,235,5,1292-1298,"W.E. Pricer, B.L. Horecker",en
+347,60SCH/RAT,13748745.0,10.1016/S0021-9258(18)64515-6,,['Free Energy Changes of the Argininosuccinate Synthetase Reaction and of the Hydrolysis of the Inner Pyrophosphate Bond of Adenosine Triphosphate'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,235,12,3597-3602,"Auguste Schuegraf, S. Ratner, Robert C. Warner",en
+348,60VOL,,10.1016/S0021-9258(19)76838-0,,['Purification and Properties of Phosphoarabinoisomerase from Propionibacterium pentosaceum'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,235,6,1550-1553,Wesley A. Volk,en
+349,61ALE,13682344.0,10.1128/jb.81.6.903-910.1961,,['CHARACTERISTICS OF CELLOBIOSE PHOSPHORYLASE'],3.1.2020,American Society for Microbiology,https://journals.asm.org/non-commercial-tdm-license,journal-article,81,6,903-910,James K. Alexander,en
+350,61ATK/BUR,13684980.0,10.1042/bj0780813,,-,-,-,-,-,-,-,-,-,-
+351,61ATK/JOH,13684982.0,10.1042/bj0790012,,-,-,-,-,-,-,-,-,-,-
+352,61BEN/SCH,,10.1016/S0021-9258(18)64053-0,,['A Phosphoglucomutase Specific for β-Glucose 1-Phosphate'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,236,8,2186-2189,"Ruth Ben-Zvi, Michael Schramm",en
+353,61BER/BER,,10.1016/S0021-9258(19)63293-X,,['The Enzymic Synthesis of Amino Acyl Derivatives of Ribonucleic Acid'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,236,6,1726-1734,"Paul Berg, Fred H. Bergmann, E.J. Ofengand, M. Dieckmann",en
+354,61CAN,,,,-,-,-,-,-,-,-,-,-,-
+355,61DAT/RAC,13719876.0,10.1016/S0021-9258(18)64277-2,,['Mechanism of Action of Transketolase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,236,3,617-623,"Asoke G. Datta, Efraim Racker",en
+356,61DOU,,,,-,-,-,-,-,-,-,-,-,-
+357,61DOU/MER,,,,-,-,-,-,-,-,-,-,-,-
+358,61GAW/GLA,13897360.0,10.1016/0003-9861(61)90136-9,,['Kinetics of the chymotrypsin-catalyzed condensation of N-benzoyl-l-tyrosine with glycylanilide'],10.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,95,2,203-210,"Oscar Gawron, A.J. Glaid, R.E. Boyle, Gerald Odstrchel",en
+359,61GOT/KOR,13900766.0,10.1042/bj0810273,,-,-,-,-,-,-,-,-,-,-
+360,61KLE,,,,-,-,-,-,-,-,-,-,-,-
+361,61KOR/GLA,13753209.0,10.1016/S0021-9258(19)63304-1,,['The Enzymatic Synthesis of Thymidine-linked Sugars'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,236,6,1791-1794,"Stuart Kornfeld, Luis Glaser",en
+362,61KRA/VEN,13753903.0,10.1016/S0021-9258(18)64442-4,,['The Equilibrium Constant of the Dihydroorotic Dehydrogenase Reaction'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,236,1,142-144,"Gladys Krakow, Birgit Vennesland",en
+363,61LED,14463407.0,10.1016/S0021-9258(19)76430-8,,['The Enzymatic Synthesis of Thiamine Monophosphate'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,236,11,3066-3071,Irwin G. Leder,en
+364,61MAH,,,,-,-,-,-,-,-,-,-,-,-
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+366,61RAC,,,,-,-,-,-,-,-,-,-,-,-
+367,61RAC2,,,,-,-,-,-,-,-,-,-,-,-
+368,61RAW/WAD,,10.1021/ja01476a003,,-,-,-,-,-,-,-,-,-,-
+369,61SAN/ZIN,13746411.0,10.1016/0003-9861(61)90070-4,,['l-Leucine dehydrogenase of Bacillus cereus'],10.2.2005,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,94,3,430-435,"B.D. Sanwal, M.W. Zink",en
+370,61VEN/RAC,13780711.0,10.1016/S0021-9258(18)64098-0,,['Mechanism of Action of Transaldolase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,236,7,1876-1882,"R. Venkataraman, Efraim Racker",en
+371,61VLA/KOM,13781723.0,,,-,-,-,-,-,-,-,-,-,-
+372,61WIL/WIL,13785328.0,10.1016/0003-9861(61)90318-6,,['Partial purification of bacterial aspartase by starch electrophoresis'],7.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,93,1,80-84,"Jack S. Wilkinson, Virginia R. Williams",en
+373,61WOO/STJ,13786500.0,10.1073/pnas.47.3.289,,-,-,-,-,-,-,-,-,-,-
+374,61YAM,14008731.0,10.1016/S0021-9258(19)76425-4,,['The Phosphorolysis of Nucleosides by Rabbit Bone Marrow'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,236,11,3043-3046,Esther W. Yamada,en
+375,62AKA/CAM,16561978.0,10.1128/jb.84.6.1194-1201.1962,,['STUDIES ON THERMOPHILIC SULFATE-REDUCING BACTERIA III'],3.1.2020,American Society for Microbiology,https://journals.asm.org/non-commercial-tdm-license,journal-article,84,6,1194-1201,"J. M. Akagi, L. Leon Campbell",en
+376,62BES,,10.1016/0076-6879(63)06160-7,,-,-,-,-,-,-,-,-,-,-
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+378,62BRU/JOU,13874013.0,10.1016/S0021-9258(19)73772-7,,['The Sialic Acids'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,237,8,2447-2453,"Paolo Brunetti, George W. Jourdian, Saul Roseman",en
+379,62CHA/VEI,13877918.0,10.1016/S0021-9258(18)60275-3,,['Pentose Metabolism in Candida'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,237,4,1014-1020,"M. Chakravorty, L.A. Veiga, Metry Bacila, B.L. Horecker",en
+380,62COM/ROS,,10.1016/S0076-6879(62)05246-5,appears in part 6,-,-,-,-,-,-,-,-,-,-
+381,62DOU/SHU,,,,-,-,-,-,-,-,-,-,-,-
+382,62DOU2,,10.1016/S0076-6879(62)05234-9,,-,-,-,-,-,-,-,-,-,-
+383,62DUR/RAW,,10.1016/0006-3002(62)90607-8,,-,-,-,-,-,-,-,-,-,-
+384,62ESP,,10.1016/S0021-9258(19)84491-5,,['Enzymic Synthesis of Adenosine Diphosphate Glucose from Glucose 1-Phosphate and Adenosine Triphosphate'],7.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,237,12,3577-3581,Joaquin Espada,en
+385,62GHA/HEA,13898172.0,10.1016/S0021-9258(19)73768-5,,['The Metabolism of l-Fucose'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,237,8,2427-2433,"Mohammad Ali Ghalambor, Edward C. Heath",en
+386,62GOL/WAG,,10.1016/0006-3002(62)91048-X,,['Enzyme systems in the mycobacteria XIII. Glycine dehydrogenase and the glyoxylic acid cycle'],4.4.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,65,2,297-306,"Dexter S. Goldman, Marion J. Wagner",en
+387,62GRI,,10.1016/S0076-6879(62)05210-6,,-,-,-,-,-,-,-,-,-,-
+388,62HAL/FEN,13903809.0,10.1016/S0021-9258(19)63410-1,,['Some Enzymic Properties of Mitochondrial Propionyl Carboxylase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,237,7,2140-2147,"Donald R. Halenz, Jan-Yung Feng, Carman S. Hegre, M. Daniel Lane",en
+389,62HAY/NIS,,10.1016/S0076-6879(62)05297-0,,-,-,-,-,-,-,-,-,-,-
+390,62HIM/RAB,13907490.0,10.1016/S0021-9258(18)60249-2,,['Formyltetrahydrofolate Synthetase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,237,9,2903-2914,"Richard H. Himes, Jesse C. Rabinowitz",en
+391,62HOR,,10.1016/S0076-6879(62)05212-X,,-,-,-,-,-,-,-,-,-,-
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+393,62KRE/MEL,14459507.0,10.1042/bj0820096,,-,-,-,-,-,-,-,-,-,-
+394,62MEN,14472566.0,10.1016/S0021-9258(18)81380-1,,['Phosphorylation of Cytidine Monophosphate in Animal Tissues'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,237,1,165-169,Joseph Mendicino,en
+395,62PET,,10.1016/S0076-6879(62)05327-6,,-,-,-,-,-,-,-,-,-,-
+396,62RAB,,,should this be 62RAZ? appears in part 2,-,-,-,-,-,-,-,-,-,-
+397,62RAT,,10.1016/S0076-6879(62)05324-0,should this be 62RAB? appears in part 2,-,-,-,-,-,-,-,-,-,-
+398,62RAV/WOL,14490617.0,10.1021/bi00908a012,,-,-,-,-,-,-,-,-,-,-
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+400,62SEG/BEA,,10.1016/S0021-9258(19)73958-1,,['Purification and Properties of Liver Glutamic-Alanine Transaminase from Normal and Corticoid-treated Rats'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,237,6,1914-1920,"H.L. Segal, Diana S. Beattie, Sarah Hopper",en
+401,62SHU/DOU,13912428.0,10.1016/S0021-9258(18)93969-4,,['A Cold-sensitive d(-)β-Hydroxybutyric Acid Dehydrogenase from Rhodospirillum rubrum'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,237,2,603-607,"C.W. Shuster, Michael Doudoroff",en
+402,62SIL,,10.1016/S0076-6879(62)05314-8,,-,-,-,-,-,-,-,-,-,-
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+405,62WIL/SNE,14001018.0,10.1016/S0021-9258(18)50139-3,,['Metabolism of α-Methylserine'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,237,10,3171-3179,"Edith M. Wilson, Esmond E. Snell",en
+406,63ALL/KEL,14012144.0,10.1016/S0021-9258(18)81114-0,,"['The Isolation, Purification, and Properties of Methylmalonyl Racemase']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,238,5,1637-1642,"S.H.G. Allen, R. Kellermeyer, Rune Stjernholm, Birgit Jacobson, Harland G. Wood",en
+407,63BEC/LEV,13970089.0,10.1016/S0021-9258(18)81322-9,,"['Purification, Kinetics, and Repression Control of Bacterial Trans-N-deoxyribosylase']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,238,2,702-709,"William S. Beck, Myron Levin",en
+408,63BER/HOL,14087284.0,,,-,-,-,-,-,-,-,-,-,-
+409,63CHE/RAW,,10.1016/0006-3002(63)91239-3,,-,-,-,-,-,-,-,-,-,-
+410,63DAY/WIL,,10.1016/0006-3002(63)90519-5,,-,-,-,-,-,-,-,-,-,-
+411,63DEV/GOU,,10.1016/0926-6550(63)90451-1,,-,-,-,-,-,-,-,-,-,-
+412,63DOB/DEM,,10.1016/0006-3002(63)90547-X,,-,-,-,-,-,-,-,-,-,-
+413,63DOM/ZEC,14095156.0,,,-,-,-,-,-,-,-,-,-,-
+414,63EDM/WRI,14109183.0,10.1016/S0021-9258(19)75304-6,,['Mannitol Dehydrogenase from Agaricus campestris'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,238,11,3539-3541,"John M. Edmundowicz, John C. Wriston",en
+415,63EHR/MAR,14109209.0,10.1016/S0021-9258(19)75330-7,,['Enzymatic Synthesis of γ-Glutamylhydroxamic Acid from Glutamic Acid and Hydroxylamine'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,238,11,3711-3716,"Elvera Ehrenfeld, Sara Jo Marble, Alton Meister",en
+416,63FLA,,10.1016/0076-6879(63)06157-7,,-,-,-,-,-,-,-,-,-,-
+417,63FRI/SCH,13963148.0,10.1016/S0021-9258(19)68001-4,,['Properties of Partially Purified Carnitine Acetyltransferase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,238,7,2509-2517,"Irving B. Fritz, Suzzanne K. Schultz, Paul A. Srere",en
+418,63GRE,,10.1016/0076-6879(63)06194-2,,-,-,-,-,-,-,-,-,-,-
+419,63HAR/COL,14063286.0,10.1016/S0021-9258(18)67880-9,,['The Citritase of Streptococcus diacetilactis'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,238,8,2648-2653,"R.J. Harvey, E.B. Collins",en
+420,63HIN/WOL,14075112.0,10.1021/bi00904a025,,-,-,-,-,-,-,-,-,-,-
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+423,63KUR/FUK,,10.1016/0006-3002(63)91027-8,,['The metabolism of γ-hydroxyglutamate in rat liver I. Enzymic synthesis of γ-hydroxy-α-ketoglutarate from pyruvate and glyoxylate'],10.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,78,4,617-628,"Kazuoki Kuratomi, Keiko Fukunaga",en
+424,63MAP/ISH,13932735.0,10.1042/bj0860173,,-,-,-,-,-,-,-,-,-,-
+425,63MAR/BAR,,10.1016/S0021-9258(18)81106-1,,['A Specific Mannitol Dehydrogenase from Lactobacillus brevis'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,238,5,1598-1603,"G. Martinez, H.A. Barker, B.L. Horecker",en
+426,63MAT/HUE,14085400.0,10.1016/S0021-9258(18)48686-3,,['Further Studies on Dihydrofolic Reductase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,238,10,3436-3442,"C.K. Mathews, F.M. Huennekens",en
+427,63MEI/BUK,14087295.0,,,-,-,-,-,-,-,-,-,-,-
+428,63MON/WHI,13936004.0,10.1016/S0021-9258(18)81333-3,,['Purification and Properties of a Sheep Liver 21-Hydroxysteroid Nicotinamide Adenine Dinucleotide Oxidoreductase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,238,2,767-774,"Carl Monder, Abraham White",en
+429,63OKA,,10.1093/oxfordjournals.jbchem.a127721,,-,-,-,-,-,-,-,-,-,-
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+431,63SCO/DUN,14086726.0,10.1016/S0021-9258(18)51808-1,,['Purification and Properties of Glutathione Reductase of Human Erythrocytes'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,238,12,3928-3933,"Edward M. Scott, Irma W. Duncan, Virginia Ekstrand",en
+432,63SLY/STA,14063285.0,10.1016/S0021-9258(18)67879-2,,['Formate Metabolism'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,238,8,2639-2647,"William S. Sly, E.R. Stadtman",en
+433,63VIL/LAR,,10.1016/0076-6879(63)06186-3,,-,-,-,-,-,-,-,-,-,-
+434,64ADA/NOR,14189888.0,10.1016/S0021-9258(18)91347-5,,['Purification and Properties of Inducible Hydroxyproline 2-Epimerase from Pseudomonas'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,239,5,1525-1535,"Elijah Adams, Isabel L. Norton",en
+435,64ASP/JAK,14154441.0,10.1016/S0021-9258(18)51644-6,,['l-Threonic Acid Dehydrogenase: Purification and Properties'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,239,3,710-713,"Anita J. Aspen, William B. Jakoby",en
+436,64AVI,14257584.0,10.1016/S0021-9258(18)91180-4,,['Sucrose-Uridine Diphosphate Glucosyltransferase from Jerusalem Artichoke Tubers'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,239,11,3613-3618,Gad Avigad,en
+437,64BAR/ROO,14245371.0,10.1016/S0021-9258(18)97713-6,,['The Glutamate Mutase System'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,239,10,3260-3266,"H.A. Barker, V. Rooze, F. Suzuki, A.A. Iodice",en
+438,64BOJ/GAU,14102876.0,10.1128/jb.87.1.75-80.1964,,['OXAMIC TRANSCARBAMYLASE OF\n STREPTOCOCCUS ALLANTOICUS'],3.1.2020,American Society for Microbiology,https://journals.asm.org/non-commercial-tdm-license,journal-article,87,1,75-80,"R. Bojanowski, Elizabeth Gaudy, R. C. Valentine, R. S. Wolfe",en
+439,64HEN/CLE,14155095.0,10.1021/bi00891a007,,-,-,-,-,-,-,-,-,-,-
+440,64IMA/MOR,,10.1093/oxfordjournals.jbchem.a127970,,-,-,-,-,-,-,-,-,-,-
+441,64KEL/ALL,14235536.0,10.1016/S0021-9258(18)93888-3,,['Methylmalonyl Isomerase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,239,8,2562-2569,"R.W. Kellermeyer, S.H.G. Allen, Rune Stjernholm, Harland G. Wood",en
+442,64LOW/PAS,14114860.0,10.1016/S0021-9258(18)51741-5,,['The Relationships between Substrates and Enzymes of Glycolysis in Brain'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,239,1,31-42,"Oliver H. Lowry, Janet V. Passonneau",en
+443,64MAI/DEK,14193832.0,10.1016/S0021-9258(18)91340-2,,['Purification and Properties of Rat Liver 2-Keto-4-hydroxyglutarate Aldolase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,239,5,1485-1491,"Umadas Maitra, Eugene E. Dekker",en
+444,64MCN/DAM,14247682.0,10.1016/S0021-9258(18)91169-5,,['Tetraoxypteridine Isomerase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,239,12,4272-4279,"Walter S. McNutt, Shridhar P. Damle",en
+445,64MEL/WOO,14245410.0,10.1016/S0021-9258(18)97752-5,,['The Mechanism of 2-Keto-3-deoxy-6-phosphogluconic Aldolase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,239,10,3511-3514,"H.P. Meloche, W.A. Wood",en
+446,64MIL/AVI,,10.1002/ijch.196400064,,-,-,-,-,-,-,-,-,-,-
+447,64MOO/REI,14245401.0,10.1016/S0021-9258(18)97743-4,,['Enzymatic Synthesis of Deoxyribonucleotides'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,239,10,3445-3452,"E. Colleen Moore, Peter Reichard, Lars Thelander",en
+448,64NOR,,10.1016/0926-6569(64)90103-8,,['Palmityl-coa:carnitine palmityltransferase'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,89,1,95-108,Kaare R. Norum,en
+449,64PRE/WOO,14245350.0,10.1016/S0021-9258(18)97692-1,,['Sugar Nucleotide Reactions in Arthrobacter'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,239,10,3119-3126,"Jack Preiss, Eileen Wood",en
+450,64ROS/RAP,,10.1038/201185a0,,['Reduction-potential of Glutathione'],5.7.2006,Springer Science and Business Media LLC,http://www.springer.com/tdm,journal-article,201,4915,185-185,"J. ROST, S. RAPOPORT",en
+451,64SAT/TSU,,10.1246/nikkashi1898.67.5_683,,-,-,-,-,-,-,-,-,-,-
+452,64TAK/SAW,,10.1016/0926-6569(64)90263-9,,['The metabolism of l-rhamnose in escherichia coli'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,92,1,10-17,"Yasuyuki Takagi, Hideo Sawada",en
+453,64WIL/HOG,14235524.0,10.1016/S0021-9258(18)93876-7,,['The Enzymes of the Galactose Operon in Escherichia coli'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,239,8,2469-2481,"David B. Wilson, David S. Hogness",en
+454,64ZAN/BAC,14127579.0,10.1128/JB.87.3.614-618.1964,,['FRUCTOSE-6-PHOSPHATE REDUCTASE FROM\n SALMONELLA GALLINARUM'],3.1.2020,American Society for Microbiology,https://journals.asm.org/non-commercial-tdm-license,journal-article,87,3,614-618,"Glaci T. Zancan, Metry Bacila",en
+455,65AND/ALL,14304839.0,10.1016/S0021-9258(18)97332-1,,['Purification and Characterization of d-Lyxose Isomerase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,240,6,2367-2372,"R.L. Anderson, D.P. Allison",en
+456,65ANN/KOS,,10.1139/o65-208,,['ENZYMATIC ENOLIZATION OF OXALACETIC ACID'],17.12.2009,Canadian Science Publishing,http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining,journal-article,43,11,1887-1889,"R. G. Annett, G. W. Kosicki",en
+457,65BAH/CAT,14321375.0,10.1016/S0021-9258(18)97227-3,,"['A Thermodynamic Study of the Hydrolysis of Cytidine 2‘,3‘-Cyclic Phosphate']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,240,8,3372-3378,"James T. Bahr, Renata E. Cathou, Gordon G. Hammes",en
+458,65BES/HER,14253449.0,10.1016/S0021-9258(18)97668-4,,['The Enzymology of Virus-infected Bacteria'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,240,1,439-445,"Maurice J. Bessman, Susan T. Herriott, Mary Jane Van Bibber Orr",en
+459,65BOY/BAR,,10.1021/bi00885a020,,-,-,-,-,-,-,-,-,-,-
+460,65BUL/HAN,14321365.0,10.1016/S0021-9258(18)97216-9,,['Kinetics of Beef Heart Glutamic-Alanine Transaminase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,240,8,3283-3294,"Bernard Bulos, Philip Handler",en
+461,65CAN/FOC,14321360.0,10.1016/S0021-9258(18)97211-X,,['Metabolism of Propionic Acid in Animal Tissues'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,240,8,3249-3257,"J.J.B. Cannata, Aldo Focesi, Rajarshi Mazumder, Robert C. Warner, Severo Ochoa",en
+462,65CAR/KIR,,10.1016/S0926-6593(65)80047-9,,['The papain-catalyzed synthesis of hippuryl anilide II. Variation of rate with substrate concentration and determination of the equilibrium constant'],4.9.2009,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,110,2,399-413,"R.P. Carty, D.M. Kirschenbaum",en
+463,65CHI/FEI,,10.1016/0006-291X(65)90155-5,,['Substrate specificity of L-rhamnulose 1-phosphate aldolase'],30.10.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,19,4,511-516,"T.H. Chiu, David Sidney Feingold",en
+464,65DAW/DIC,14346088.0,10.1042/bj0940353,,-,-,-,-,-,-,-,-,-,-
+465,65EIC/CYN,14285233.0,10.1021/bi00877a024,,-,-,-,-,-,-,-,-,-,-
+466,65GAU/WOL,5854583.0,10.1128/jb.90.6.1531-1536.1965,,['Ureidoglycolate Synthetase of\n Streptococcus allantoicus\n II. Properties of the Enzyme and Reaction Equilibrium'],3.1.2020,American Society for Microbiology,https://journals.asm.org/non-commercial-tdm-license,journal-article,90,6,1531-1536,"Elizabeth T. Gaudy, R. S. Wolfe",en
+467,65GHO/ROS,14285487.0,10.1016/S0021-9258(18)97467-3,,['The Sialic Acids'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,240,4,1525-1530,"Sudhamoy Ghosh, Saul Roseman",en
+468,65GHO/ROS2,14285488.0,10.1016/S0021-9258(18)97468-5,,['The Sialic Acids'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,240,4,1531-1536,"Sudhamoy Ghosh, Saul Roseman",en
+469,65ICH/HIR,,10.1271/nogeikagaku1924.39.291,,-,-,-,-,-,-,-,-,-,-
+470,65KAT/BUC,14275142.0,10.1016/S0021-9258(17)45250-1,,['Enzymatic Synthesis of the Methyl Group of Methionine'],4.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,240,2,825-835,"Howard M. Katzen, John M. Buchanan",en
+471,65KAZ/GRO,14256957.0,10.1016/S0021-9258(18)97615-5,,['Metabolism of Propionic Acid in Animal Tissues'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,240,1,64-67,"Yoshito Kaziro, Albert Grossman, Severo Ochoa",en
+472,65LEE/DOB,16562063.0,10.1128/jb.90.3.653-660.1965,,['Oxidative Metabolism in\n Pediococcus pentosaceus\n III. Glucose Dehydrogenase System'],3.1.2020,American Society for Microbiology,https://journals.asm.org/non-commercial-tdm-license,journal-article,90,3,653-660,"Chin K. Lee, Walter J. Dobrogosz",en
+473,65MAR/JEN,4953710.0,10.1016/S0021-9258(18)97177-2,,['d-Alanine-d-Glutamate Transaminase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,240,9,3538-3546,"M. Martinez-Carrion, W. Terry Jenkins",en
+474,65MAY/GIN,14299608.0,10.1016/S0021-9258(18)97402-8,,['Purification and Properties of Cytidine Diphosphate d-Glucose Pyrophosphorylase from Salmonella paratyphi A'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,240,5,1900-1904,"Robert M. Mayer, Victor Ginsburg",en
+475,65MOR/JAM,16749122.0,10.1042/bj0970037,,-,-,-,-,-,-,-,-,-,-
+476,65ONO/HIR,,10.1093/oxfordjournals.jbchem.a128147,,-,-,-,-,-,-,-,-,-,-
+477,65PIN,,10.1051/jcp/1965620591,,-,-,-,-,-,-,-,-,-,-
+478,65SEK/SUN,,,,-,-,-,-,-,-,-,-,-,-
+479,65SHA/CLE,14299613.0,10.1016/S0021-9258(18)97409-0,,"['The Partial Purification, Properties, and Mechanism of Action of Pig Liver Isopentenyl Pyrophosphate Isomerase']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,240,5,1946-1956,"Damayanti H. Shah, W.W. Cleland, John W. Porter",en
+480,65STI/DIA,,,,-,-,-,-,-,-,-,-,-,-
+481,65STR,14284729.0,10.1016/S0021-9258(18)97564-2,,['Purification and Properties of Rat Liver Ornithine δ-Transaminase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,240,3,1225-1230,Harold J. Strecker,en
+482,65TAK/HIR,,10.1093/oxfordjournals.jbchem.a128195,,-,-,-,-,-,-,-,-,-,-
+483,65TAK/YOS,,10.1093/oxfordjournals.jbchem.a128194,,-,-,-,-,-,-,-,-,-,-
+484,65TAT/DAT,14348207.0,10.1042/bj0940470,,-,-,-,-,-,-,-,-,-,-
+485,65TSU/SAT,,10.1271/bbb1961.29.1129,,-,-,-,-,-,-,-,-,-,-
+486,65UYE/RAB,14285511.0,10.1016/S0021-9258(18)97492-2,,['Metabolism of Formiminoglycine'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,240,4,1701-1710,"Kosaku Uyeda, Jesse C. Rabinowitz",en
+487,65WAL/SAL,4378782.0,10.1021/bi00882a015,,-,-,-,-,-,-,-,-,-,-
+488,65YOS,14284712.0,10.1016/S0021-9258(18)97547-2,,['Enzymic Properties of Malate Dehydrogenase of Bacillus subtilis'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,240,3,1118-1124,Akira Yoshida,en
+489,65YOS/FRE,,10.1016/0926-6593(65)90009-3,,['Enzymic properties of alanine dehydrogenase of Bacillus subtilis'],4.4.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,96,2,248-262,"Akira Yoshida, Ernst Freese",en
+490,66ALB/BAS,4287931.0,10.1016/S0021-9258(18)96559-2,,['Crystallization and Properties of Uridine Diphosphate Glucose Pyrophosphorylase from Liver'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,241,12,2968-2975,"G.J. Albrecht, S.T. Bass, L.L. Seifert, R.G. Hansen",en
+491,66ALL,4289051.0,10.1016/S0021-9258(18)96427-6,,['The Isolation and Characterization of Malate-Lactate Transhydrogenase from Micrococcus lactilyticus'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,241,22,5266-5275,S.H.G. Allen,en
+492,66AVI/ENG,4379259.0,10.1016/S0021-9258(18)96926-7,,['5-Keto-d-fructose'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,241,2,373-378,"Gad Avigad, Sasha Englard, Sharon Pifko",en
+493,66BER/MOE,5982377.0,,,-,-,-,-,-,-,-,-,-,-
+494,66CAR/HUL,16742459.0,10.1042/bj1010781,,-,-,-,-,-,-,-,-,-,-
+495,66CHA/WIL,5924646.0,10.1016/S0021-9258(18)99776-0,,['Participation of the Unsymmetrical Disulfide of Coenzyme A and Glutathione in an Enzymatic Sulfhydryl-Disulfide Interchange'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,241,18,4251-4260,"Simon H. Chang, David R. Wilken",en
+496,66DED,,10.1016/0076-6879(66)08091-1,,-,-,-,-,-,-,-,-,-,-
+497,66DOM/ZEC,,10.1016/0076-6879(66)09115-8,,-,-,-,-,-,-,-,-,-,-
+498,66GIB/MOR,16749179.0,10.1042/bj0990021p,,-,-,-,-,-,-,-,-,-,-
+499,66GOL/MAR,5901055.0,10.1016/S0021-9258(18)96955-3,,"['β-1,3-Oligoglucan:Orthophosphate Glucosyltransferase from Euglena gracilis']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,241,1,45-50,"Sara H. Goldemberg, Luis R. Maréchal, Bazilicia C. De Souza",en
+500,66HAN/ALB,,10.1016/0076-6879(66)08042-X,,-,-,-,-,-,-,-,-,-,-
+501,66HAN/VER,,10.1016/0076-6879(66)08048-0,,-,-,-,-,-,-,-,-,-,-
+502,66HOR/HEN,4287985.0,10.1016/S0021-9258(18)96478-1,,['Kinetic Studies of Adenine Phosphoribosyltransferase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,241,14,3404-3408,"Makoto Hori, J. Frank Henderson",en
+503,66JEN/DAR,5912360.0,10.1016/S0021-9258(18)96541-5,,['Glutamic-Aspartic Transaminase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,241,12,2845-2854,"W. Terry Jenkins, Linda D'Ari",en
+504,66KIM/SUZ,5933869.0,10.1016/S0021-9258(18)96808-0,,['Studies on Cytidine Diphosphate Glucose Pyrophosphorylase and Related Enzymes of Azotobacter vinelandii'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,241,5,1099-1113,"Koji Kimata, Sakaru Suzuki",en
+505,66MAR/COH,4958913.0,10.1016/S0021-9258(18)99770-X,,['A Kinetic Study of the Mechanism of Crystalline Carbamate Kinase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,241,18,4197-4208,"Margaret Marshall, Philip P. Cohen",en
+506,66MAR/WAD,5924638.0,10.1016/S0021-9258(18)99761-9,,"[""Adenosine Triphosphate-Adenosine 5'-Monophosphate Phosphotransferase of Bovine Liver Mitochondria""]",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,241,18,4136-4145,"Frank S. Markland, Charles L. Wadkins",en
+507,66MAT,5924649.0,10.1016/S0021-9258(18)99779-6,,"['Enzymatic Synthesis of Cytidine Diphosphate 3,6-Dideoxyhexoses']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,241,18,4275-4282,Sachiko Matsuhashi,en
+508,66MAT/STR,,10.1016/0076-6879(66)08061-3,,-,-,-,-,-,-,-,-,-,-
+509,66MUD/KLE,5961285.0,10.1021/bi00869a030,,-,-,-,-,-,-,-,-,-,-
+510,66MUR/SUG,5941994.0,10.1016/0003-9861(66)90153-6,,['Enzymic mechanism of starch synthesis in ripening rice grains'],25.11.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,113,1,34-44,"Takao Murata, Tatsuo Sugiyama, Takao Minamikawa, T. Akazawa",en
+511,66NAT,,10.1271/bbb1961.30.887,,-,-,-,-,-,-,-,-,-,-
+512,66REI,,10.1016/0076-6879(66)09112-2,,-,-,-,-,-,-,-,-,-,-
+513,66SCH,,10.1016/0926-6593(66)90039-7,,['Choline acetyltransferase purification and effect of salts on the mechanism of the enzyme-catalyzed reaction'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,122,3,470-481,Jan Schuberth,en
+514,66SCH/HOR,4381350.0,10.1016/0003-9861(66)90020-8,,-,-,-,-,-,-,-,-,-,-
+515,66SHU,,10.1016/0076-6879(66)09104-3,,-,-,-,-,-,-,-,-,-,-
+516,66STA/DEN,,10.1016/0926-6593(66)90144-5,,['Mechanism of arginine biosynthesis in Chlamydomonas reinhardti I. Purification and properties of ornithine acetyltransferase'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,128,1,82-91,"Maria Staub, G. Dénes",en
+517,66THO/NAN,5971743.0,10.1016/0003-9861(66)90126-3,,['Isotope and solvent effects of deuterium on aconitase'],14.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,117,1,65-74,"John F. Thomson, Sharron L. Nance, Karen J. Bush, Patricia A. Szczepanik",en
+518,66TOO/WAK,,10.1016/0005-2760(66)90001-4,,['Studies on the mechanism of fatty acid synthesis XV. Preparation and general properties of β-ketoacyl acyl carrier protein reductase from Escherichia coli'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,116,2,189-197,"Richard E. Toomey, Salih J. Wakil",en
+519,66UHR/MAR,5954807.0,10.1016/S0021-9258(18)96447-1,,['Studies on Adenosine Triphosphate: Arginine Phosphotransferase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,241,22,5428-5435,"Marie Louise Uhr, Frank Marcus, J.F. Morrison",en
+520,66VER/ROD,5946626.0,10.1016/S0021-9258(18)96658-5,,['Purification and Properties of Guanosine Diphosphate Hexose Pyrophosphorylase from Mammalian Tissues'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,241,9,2007-2013,"H. Verachtert, P. Rodriguez, S.T. Bass, R.G. Hansen",en
+521,66WIL/WAK,5330116.0,10.1016/S0021-9258(18)96625-1,,['Studies on the Mechanism of Fatty Acid Synthesis'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,241,10,2326-2332,"I.P. Williamson, Salih J. Wakil",en
+522,66WOO/DAV,4288897.0,10.1016/S0021-9258(18)96399-4,,"['The Equilibria of Reactions Catalyzed by Carboxytransphosphorylase, Carboxykinase, and Pyruvate Carboxylase and the Synthesis of Phosphoenolpyruvate']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,241,23,5692-5704,"Harland G. Wood, Judith J. Davis, Hans Lochmüller",en
+523,67BAR,,10.1007/BF00406311,,['Citramalate lyase of Clostridium tetanomorphum'],8.11.2004,Springer Science and Business Media LLC,http://www.springer.com/tdm,journal-article,59,1-3,4-12,H. A. Barker,en
+524,67DAN/YOS,,10.1271/bbb1961.31.284,,-,-,-,-,-,-,-,-,-,-
+525,67ENG/DAL,4384597.0,10.1042/bj1050691,,-,-,-,-,-,-,-,-,-,-
+526,67ENG/DEN,5583983.0,10.1042/bj1050032c,,-,-,-,-,-,-,-,-,-,-
+527,67EPP/DAW,6016604.0,10.1016/S0021-9258(19)81449-7,,['The Comparative Enzymology of Creatine Kinases'],7.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,242,2,204-209,"Hans M. Eppenberger, David M. Dawson, Nathan O. Kaplan",en
+528,67GRO,6016328.0,10.1016/S0021-9258(18)96331-3,,['Deoxyribose 5-Phosphate Aldolase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,242,1,155-159,D.P. Groth,en
+529,67HER/JEN,,10.1016/S0021-9258(18)95886-2,,['Coenzyme A Transferase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,242,15,3468-3480,"Louis B. Hersh, William P. Jencks",en
+530,67HIR/GRE,6022873.0,10.1016/S0021-9258(18)96047-3,,['Studies on Phosphoserine Aminotransferase of Sheep Brain'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,242,9,2283-2287,"Helga Hirsch, David M. Greenberg",en
+531,67KEP/TOV,5633396.0,10.1016/S0021-9258(18)99355-5,,['Biohydrogenation of Unsaturated Fatty Acids'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,242,24,5686-5692,"Carol R. Kepler, S.B. Tove",en
+532,67LOM/GRE,6033708.0,10.1016/0003-9861(67)90352-9,,"['Studies on N5,N10-methenyltetrahydrofolate cyclohydrolase']",27.10.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,118,2,297-304,"Leon Lombrozo, David M. Greenberg",en
+533,67MOR/WHI,6079774.0,10.1111/j.1432-1033.1967.tb19509.x,,['Isotope Exchange Studies of the Reaction Catalyzed by ATP: Creatine Phosphotransferase'],4.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,3,2,145-152,"J. F. Morrison, A. White",en
+534,67PLO/CLE,6061708.0,10.1016/S0021-9258(18)95802-3,,['Purification and Kinetic Studies of the Citrate Cleavage Enzyme'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,242,18,4239-4247,"K.M. Plowman, W.W. Cleland",en
+535,67POE/GUT,4294746.0,10.1016/0003-9861(67)90140-3,,['Kinetic studies of temperature changes and oxygen uptake in a differential calorimeter: The heat of oxidation of NADH and succinate'],14.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,122,1,204-211,"Martin Poe, H. Gutfreund, Ronald W. Estabrook",en
+536,67ROS/ADA,12325368.0,10.1016/S0021-9258(18)99389-0,,['4-Hydroxy-2-ketoglutarate Aldolase of Rat Liver'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,242,23,5524-5534,"Ronal G. Rosso, Elijah Adams",en
+537,67SAK/YOR,,10.1271/bbb1961.31.525,,-,-,-,-,-,-,-,-,-,-
+538,67SAK/YOR2,,10.1271/bbb1961.31.533,,-,-,-,-,-,-,-,-,-,-
+539,67SIL/VOE,4381552.0,10.1016/S0021-9258(18)96185-5,,['Purification and Mechanism of Action of Sucrose Phosphorylase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,242,6,1338-1346,"Richard Silverstein, Judith Voet, Dan Reed, Robert H. Abeles",en
+540,67SOD/OSU,,10.1271/bbb1961.31.1097,,-,-,-,-,-,-,-,-,-,-
+541,67TAK,,10.1271/bbb1961.31.309,,-,-,-,-,-,-,-,-,-,-
+542,67TAK/HIZ,,10.1016/0005-2744(67)90241-0,,['Crystallization and properties of pea glucosephosphate isomerase'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,146,2,568-575,"Yasuhito Takeda, Susumu Hizukuri, Ziro Nikuni",en
+543,67TAK2,,10.1271/bbb1961.31.435,,-,-,-,-,-,-,-,-,-,-
+544,67TRI/VOG,,10.1016/0005-2744(67)90197-0,,['Allantoate and ureidoglycolate degradation by Pseudomonas aeruginosa'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,132,1,115-126,"F. Trijbels, G.D. Vogels",en
+545,67UYE/RAB,4383631.0,10.1016/S0021-9258(18)99549-9,,['Enzymes of Clostridial Purine Fermentation'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,242,19,4378-4385,"Kosaku Uyeda, Jesse C. Rabinowitz",en
+546,67WIL/HIR,,10.1016/0005-2744(67)90139-8,,['Reversibility of the “irreversible” histidine ammonia-lyase reaction'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,139,1,214-216,"Virginia R. Williams, Janice M. Hiroms",en
+547,67WIL/LUN,4291787.0,10.1042/bj1030514,,-,-,-,-,-,-,-,-,-,-
+548,67WOL,6061417.0,10.1016/S0021-9258(18)99514-1,,['The Free Energy of Hydrolysis of Adenosine to Inosine and Ammonia'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,242,20,4711-4714,Richard Wolfenden,en
+549,67WU/WIT,,10.1021/ja00985a003,,-,-,-,-,-,-,-,-,-,-
+550,68AUR/KLE,4302217.0,10.1111/j.1432-1033.1968.tb00437.x,,['Reinigung und Eigenschaften der Carnitindehydrogenase aus Pseudomonas aeruginosa'],3.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,6,2,196-201,"H. Aurich, H.‐P. Kleber, H. Sorger, H. Tauchert",en
+551,68AVI/ALR,4384672.0,10.1016/S0021-9258(18)93531-3,,['Purification and Properties of a Nicotinamide Adenine Dinucleotide Phosphate-linked Aldohexose Dehydrogenase from Gluconobacter cerinus'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,243,8,1936-1941,"G Avigad, Y Alroy, S Englard",en
+552,68AYL/SNE,5650370.0,10.1021/bi00845a002,,-,-,-,-,-,-,-,-,-,-
+553,68AYL/SNE2,5650371.0,10.1021/bi00845a003,,-,-,-,-,-,-,-,-,-,-
+554,68BAD/MIL,5681454.0,10.1021/bi00850a014,,-,-,-,-,-,-,-,-,-,-
+555,68BEE/DEL,,10.1111/j.1432-1033.1968.tb00453.x,,['Hexopyranoside: Cytochrome c Oxidoreductase from Agrobacterium tumefaciens'],3.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,6,3,331-343,"J. van Beeumen, J. de Ley",en
+556,68BOM/PRA,,10.1016/0005-2728(68)90105-9,,"['Study of adenosine 5′-mono-, di- and triphosphates in plant tissues. IV. Regulation of the level of nucleotides, in vivo, by adenylate kinase: Theoretical and experimental study']",11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,162,2,230-242,"Jean-Loup Bomsel, Alain Pradet",en
+557,68BRO,,,,-,-,-,-,-,-,-,-,-,-
+558,68BUR/WAL,,10.1016/0005-2744(68)90028-4,,['Kinetics of triose phosphate isomerase'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,151,3,714-715,"P.M. Burton, S.G. Waley",en
+559,68DYS/NOL,5647261.0,10.1016/S0021-9258(18)93559-3,,['The Effect of pH and Temperature on the Kinetic Parameters of Phosphoglucose Isomerase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,243,7,1401-1414,"J E D Dyson, E A Noltmann",en
+560,68ERI,,10.1111/j.1365-2621.1968.tb03667.x,,['Alcohol: NAD Oxidoreductase (E. C. 1.1.1.1.) from Peas'],26.8.2006,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,33,5,525-532,C. E. ERIKSSON,en
+561,68HAT/SLA,4305612.0,10.1042/bj1060141,,-,-,-,-,-,-,-,-,-,-
+562,68HAV/HAN,5655435.0,10.1021/bi00845a039,,-,-,-,-,-,-,-,-,-,-
+563,68JEA/DEM,,10.1139/m68-068,,['Indolelactate dehydrogenase from Clostridium sporogenes'],8.2.2010,Canadian Science Publishing,http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining,journal-article,14,4,429-435,"Marcel Jean, R. D. DeMoss",en
+564,68KOH,4300866.0,10.1016/S0021-9258(18)93210-2,,['Tartaric Acid Metabolism'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,243,17,4426-4433,L D Kohn,en
+565,68KOH/JAK,4297260.0,10.1016/S0021-9258(18)93399-5,,['Tartaric Acid Metabolism'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,243,10,2472-2478,"L D Kohn, W B Jakoby",en
+566,68KOH/JAK2,4385076.0,10.1016/S0021-9258(18)93401-0,,['Tartaric Acid Metabolism'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,243,10,2486-2493,"L D Kohn, W B Jakoby",en
+567,68LON/DAL,4387224.0,10.1042/bj1100217,,-,-,-,-,-,-,-,-,-,-
+568,68MAY/AND,5726889.0,10.1016/S0021-9258(18)93144-3,,['Pathway of L-Mannose Degradation in Aerobacter aerogenes'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,243,24,6330-6333,"J W Mayo, R L Anderson",en
+569,68MIZ/WEE,5658542.0,10.1016/S0021-9258(19)34190-0,,['Studies on the Mechanism of Fatty Acid Synthesis'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,243,13,3661-3670,"M Mizugaki, G Weeks, R E Toomey, S J Wakil",en
+570,68NIX/BLA,5687716.0,10.1016/S0021-9258(18)93178-9,,['Dihydrofolate Reductase of Streptococcus faecium'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,243,18,4722-4731,"P F Nixon, R L Blakley",en
+571,68POT/GLO,5690817.0,10.1016/S0021-9258(18)92023-5,,['Choline Acetyltransferase from Rat Brain'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,243,14,3864-3870,"L T Potter, V A S Glover, J K Saelens",en
+572,68REE/MEN,4302788.0,10.1016/S0021-9258(18)91972-1,,['The Pyruvate-Phosphate Dikinase Reaction'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,243,20,5486-5491,"R E Reeves, R A Menzies, D S Hsu",en
+573,68SAL/NOR,,10.1016/0005-2744(68)90116-2,,['The specificity of UDP-glucose 4-epimerase from the yeast Saccharomyces fragilis'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,151,2,484-492,"W.L. Salo, J.H. Nordin, D.R. Peterson, R.D. Bevill, S. Kirkwood",en
+574,68SU/RUS,5661709.0,10.1016/S0021-9258(18)92018-1,,"[""Adenylate Kinase from Bakers' Yeast""]",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,243,14,3826-3833,"S Su, P J Russell",en
+575,68SUG/PIZ,4384871.0,10.1016/S0021-9258(18)93450-2,,['The Mechanism of End Product Inhibition of Serine Biosynthesis'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,243,9,2081-2089,"E Sugimoto, L I Pizer",en
+576,68TAN/KAN,5655499.0,10.1111/j.1432-1033.1968.tb00199.x,,"['Myo‐Inositol, a Cofactor in the Biosynthesis of Stachyose']",4.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,4,2,233-239,"W. TANNER, O. KANDLER",en
+577,68VEE,,,,-,-,-,-,-,-,-,-,-,-
+578,69ALB,,10.1016/S0021-9258(18)93127-3,,"['Standard Gibbs Free Energy, Enthalpy, and Entropy Changes as a Function of pH and pMg for Several Reactions Involving Adenosine Phosphates']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,244,12,3290-3302,R A Alberty,en
+579,69BAR,,,,-,-,-,-,-,-,-,-,-,-
+580,69BEN,,,,-,-,-,-,-,-,-,-,-,-
+581,69BLA,5781279.0,10.1111/j.1432-1033.1969.tb00526.x,,['Magnesium and the Aconitase Equilibrium: Determination of Apparent Stability Constants of Magnesium Substrate Complexes from Equilibrium Data'],4.3.2005,Wiley,http://doi.wiley.com/10.1002/tdm_license_1.1,journal-article,8,2,287-291,J. McD. Blair,en
+582,69BLA/FRA,5824560.0,10.1016/S0021-9258(18)94283-3,,['Thyroidal Phenylpyruvate Tautomerase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,244,18,4864-4870,"F Blasi, F Fragomele, I Covelli",en
+583,69BRE/AAS,,,,-,-,-,-,-,-,-,-,-,-
+584,69DAH/AND,,10.1016/0006-291X(69)90681-0,,['2-Keto-3-deoxy-L-arabonate aldolase and its role in A new pathway of L-arabinose degradation'],30.10.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,36,5,809-814,"A.Stephen Dahms, R.L. Anderson",en
+585,69DOL,4310090.0,10.1016/S0021-9258(18)63657-9,,['Kinetics of Malic-Lactic Transhydrogenase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,244,19,5273-5285,M.I. Dolin,en
+586,69FAN/FEI,16657106.0,10.1104/pp.44.4.599,,['Nucleoside Diphosphate-sugar 4-Epimerases I. Uridine Diphosphate Glucose 4-Epimerase of Wheat Germ'],13.12.2008,Oxford University Press (OUP),http://aspb.org/publications/aspb-journals/open-articles,journal-article,44,4,599-604,"Der-Fong Fan, David Sidney Feingold",en
+587,69GAR/CLE,5793714.0,10.1021/bi00830a026,,-,-,-,-,-,-,-,-,-,-
+588,69GEO/TRA,,,,-,-,-,-,-,-,-,-,-,-
+589,69GRE/RUD,4309154.0,10.1016/S0021-9258(18)93695-1,,"['Enthalpy of Hydrolysis of the 3′ Bond of Adenosine 3′, 5′-Monophosphate and Guanosine 3′, 5′-Monophosphate']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,244,17,4798-4800,"P Greengard, S A Rudolph, J M Sturtevant",en
+590,69KLO,,10.1016/0076-6879(69)13065-7,,-,-,-,-,-,-,-,-,-,-
+591,69LAN/DEK,4309127.0,10.1021/bi00835a041,,-,-,-,-,-,-,-,-,-,-
+592,69PAS/LOW,5814030.0,10.1016/S0021-9258(18)91871-5,,"['Glucose 1,6-Diphosphate Formation by Phosphoglucomutase in Mammalian Tissues']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,244,4,902-909,"J V Passonneau, O H Lowry, D W Schulz, J G Brown",en
+593,69PET/MCK,4306134.0,10.1016/0003-9861(69)90128-3,,['Enzymic ω-oxidation: Stoichiometry of the ω-oxidation of fatty acids'],10.2.2005,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,131,1,245-252,"Julian A. Peterson, Eva J. McKenna, Ronald W. Estabrook, Minor J. Coon",en
+594,69POP,,10.1016/S0076-6879(69)15014-4,,-,-,-,-,-,-,-,-,-,-
+595,69ROS/HAM,5814934.0,10.1021/bi00833a017,,-,-,-,-,-,-,-,-,-,-
+596,69SHE/ALE,5773308.0,10.1016/S0021-9258(18)94451-0,,"['Purification and Properties of β-1,4-Oligoglucan: Orthophosphate Glucosyltransferase from Clostridium thermocellum']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,244,2,457-464,"K Sheth, J K Alexander",en
+597,69SMI/MOR,5800442.0,10.1016/S0021-9258(17)36405-0,,['Kinetic Studies on the Arginine Kinase Reaction'],18.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,244,15,4224-4234,"E Smith, J F Morrison",en
+598,69SWI,4306285.0,10.1016/S0021-9258(18)91705-9,,['Regulation and Mechanism of Phosphoribosylpyrophosphate Synthetase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,244,11,2854-2863,R L Switzer,en
+599,69TSU/FUK,5782905.0,10.1016/S0021-9258(18)91886-7,,['Purification and Specific Kinetic Properties of Erythrocyte Uridine Diphosphate Glucose Pyrophosphorylase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,244,4,1008-1015,"K K Tsuboi, K Fukunaga, J C Petricciani",en
+600,69VEE/EGG,4391039.0,10.1042/bj1150609a,,-,-,-,-,-,-,-,-,-,-
+601,69VEE/RAI,5357024.0,10.1042/bj1150837,,-,-,-,-,-,-,-,-,-,-
+602,69VIL/DAL,4391041.0,10.1042/bj1150633,,-,-,-,-,-,-,-,-,-,-
+603,69WAN/BAR,5769987.0,10.1016/S0021-9258(18)83432-9,,['Purification and Properties of L-Citramalate Hydrolyase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,244,10,2516-2526,"C C Wang, H A Barker",en
+604,69WHI/LEJ,4989322.0,10.1042/bj1130589,,-,-,-,-,-,-,-,-,-,-
+605,70ALB,5423264.0,10.1021/bi00814a011,,-,-,-,-,-,-,-,-,-,-
+606,70BAL/DEN,,10.1016/0076-6879(71)17212-6,,-,-,-,-,-,-,-,-,-,-
+607,70BEN/FRI,5442269.0,10.1016/S0021-9258(18)63142-4,,['Allosteric Control of Glucosamine Phosphate Isomerase from the Adult Housefly and Its Role in the Synthesis of Glucosamine 6-Phosphate'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,245,9,2219-2228,"Robert L. Benson, Stanley Friedman",en
+608,70BLA,4245368.0,10.1111/j.1432-1033.1970.tb00940.x,,"['Magnesium, Potassium, and the Adenylate Kinase Equilibrium']",4.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,13,2,384-390,J. McD. Blair,en
+609,70BRO/KRE,4316090.0,10.1042/bj1170091,,-,-,-,-,-,-,-,-,-,-
+610,70CHI/ZAP,5438361.0,10.1016/S0021-9258(19)77160-9,,"['Lysine 2,3-Aminomutase']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,245,7,1778-1789,"T.P. Chirpich, V. Zappia, R.N. Costilow, H.A. Barker",en
+611,70DEN,,10.1016/0076-6879(71)17195-9,,-,-,-,-,-,-,-,-,-,-
+612,70FAN/FEI,5483919.0,10.1104/pp.46.4.592,,['Nucleoside Diphosphate-Sugar 4-Epimerases'],13.12.2008,Oxford University Press (OUP),http://aspb.org/publications/aspb-journals/open-articles,journal-article,46,4,592-595,"Der-Fong Fan, David Sidney Feingold",en
+613,70GEO/WIT,,10.1016/0005-2728(70)90126-X,,['“Squiggle-H2O”. An enquiry into the importance of solvation effects in phosphate ester and anhydride reactions'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,223,1,1-15,"Philip George, Robert J. Witonsky, Mendel Trachtman, Clara Wu, William Dorwart, Linda Richman, William Richman, Fahd Shurayh, Barry Lentz",en
+614,70HER,5470822.0,10.1016/S0021-9258(18)62958-8,,['5-Hydroxy-N-methylpyroglutamate Synthetase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,245,14,3526-3535,Louis B. Hersh,en
+615,70HEY/ELB,5438047.0,10.1128/jb.101.3.777-780.1970,,['Purification of a\n d\n -Mannose Isomerase from\n Mycobacterium smegmatis'],3.1.2020,American Society for Microbiology,https://journals.asm.org/non-commercial-tdm-license,journal-article,101,3,777-780,"Ann Hey-Ferguson, Alan D. Elbein",en
+616,70JEN/TAY,,10.1016/0076-6879(71)17285-0,,-,-,-,-,-,-,-,-,-,-
+617,70KNO/HAN,5427280.0,10.1016/S0021-9258(18)63098-4,,['Uridine Diphosphate Glucose Pyrophosphorylase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,245,10,2499-2504,"Janice K. Knop, R.G. Hansen",en
+618,70KOH/WAR,4395378.0,10.1016/S0021-9258(18)62926-6,,['The Kinetic Properties of Spinach Leaf Glyoxylic Acid Reductase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,245,15,3831-3839,"Leonard D. Kohn, William A. Warren",en
+619,70KRI/BUC,5493986.0,10.1111/j.1432-1033.1970.tb01202.x,,['3‐Phosphoglycerate Kinase from Rabbit Sceletal Muscle and Yeast'],3.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,17,3,568-580,"Wolfgang K. G. Krietsch, Theodor Bücher",en
+620,70MAN/HOL,4910853.0,10.1073/pnas.65.3.660,,-,-,-,-,-,-,-,-,-,-
+621,70MAR/COH,,10.1016/0076-6879(71)17186-8,,-,-,-,-,-,-,-,-,-,-
+622,70NAK/FUJ,,10.1016/0005-2744(70)90054-9,,['α-Aminoadipate aminotransferase of rat liver mitochondria'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,198,2,219-228,"Y. Nakatani, M. Fujioka, K. Higashino",en
+623,70NAK/TSU,5498430.0,10.1016/S0021-9258(19)63814-7,,['Aromatic α-Keto Acid Reductase from Rat Kidney'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,245,17,4443-4449,"Minoru Nakano, Yachiyo Tsutsumi, T.S. Danowski",en
+624,70TSA/HOL,,10.1016/0003-9861(70)90347-4,,"['Purification, stabilization, and properties of bovine mammary UDP-galactose 4-epimerase']",25.11.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,136,1,233-244,"C.M. Tsai, N. Holmberg, K.E. Ebner",en
+625,70TSU/FRI,4394942.0,10.1016/S0021-9258(18)62643-2,,['Ornithine Metabolism by Clostridium sticklandii'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,245,22,5914-5926,"Yoshihisa Tsuda, Herbert C. Friedmann",en
+626,70VEE/RAI,4315932.0,10.1042/bj1170499,,-,-,-,-,-,-,-,-,-,-
+627,70WUR/HES,4395302.0,10.1515/bchm2.1970.351.2.1537,,-,-,-,-,-,-,-,-,-,-
+628,70WUR/SCH,5451283.0,10.1515/bchm2.1970.351.2.961,,-,-,-,-,-,-,-,-,-,-
+629,71BRI/CAR,5168977.0,10.1021/bi00800a028,,-,-,-,-,-,-,-,-,-,-
+630,71BRI/CLA,,,,-,-,-,-,-,-,-,-,-,-
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+632,71COH/WOL,4944312.0,10.1016/S0021-9258(19)45813-4,,['The Equilibrium of Hydrolytic Deamination of Cytidine and N4-Methylcytidine'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,246,24,7566-7568,"Robert M. Cohen, Richard Wolfenden",en
+633,71GLO/POT,,10.1111/j.1471-4159.1971.tb11987.x,,['PURIFICATION AND PROPERTIES OF CHOLINE ACETYLTRANSFERASE FROM OX BRAIN STRIATE NUCLEI'],13.12.2006,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,18,4,571-580,"V. A. S. Glover, L. T. Potter",en
+634,71HAY/GRE,4328843.0,10.1016/S0021-9258(18)61884-8,,['On the Equilibrium of the Adenylate Cyclase Reaction'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,246,18,5840-5843,"Osamu Hayaishi, Paul Greengard, Sidney P. Colowick",en
+635,71HOR/HUS,5148773.0,,,-,-,-,-,-,-,-,-,-,-
+636,71JEN/SCH,,10.1021/ja00745a017,,-,-,-,-,-,-,-,-,-,-
+637,71JOS/WAK,4934182.0,10.1016/0003-9861(71)90234-7,,['Studies on the mechanism of fatty acid synthesis'],10.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,143,2,493-505,"V.C. Joshi, Salih J. Wakil",en
+638,71KAT,4401291.0,10.1016/s0003-9861(71)80057-7,,['Sepiapterin reductase from horse liver: Purification and properties of the Enzyme'],12.7.2006,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,146,1,202-214,Setsuko Katoh,en
+639,71KUN/STA,5574401.0,10.1016/S0021-9258(18)62235-5,,['Nicotinic Acid Metabolism'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,246,10,3378-3388,"Hsiang-Fu Kung, Thressa C. Stadtman",en
+640,71MCC/CHA,5129727.0,10.1016/S0021-9258(19)45873-0,,['Purification and Properties of Carboxypeptidase G1'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,246,23,7207-7213,"J.L. McCullough, B.A. Chabner, J.R. Bertino",en
+641,71NOJ/TAN,,10.1093/oxfordjournals.jbchem.a129527,,-,-,-,-,-,-,-,-,-,-
+642,71RAJ/LUM,,10.1021/j100680a006,,-,-,-,-,-,-,-,-,-,-
+643,71ROB,5570433.0,10.1016/S0021-9258(18)61962-3,,['The Formation of Uridine Diphosphate-Glucuronic Acid in Plants'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,246,16,4995-5002,R.M. Roberts,en
+644,71RUD/JOH,4322715.0,10.1016/S0021-9258(19)76969-5,,"[""The Enthalpy of Hydrolysis of Various 3',5'- and 2',3'-Cyclic Nucleotides""]",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,246,5,1271-1273,"Stephen A. Rudolph, Edward M. Johnson, Paul Greengard",en
+645,71SHI/SUG,5552394.0,10.1111/j.1432-1033.1971.tb01312.x,,['Metabolism of Deoxyribonucleotides. Purification and Properties of Deoxyguanosine Monophosphokinase of Calf Thymus'],3.3.2005,Wiley,http://doi.wiley.com/10.1002/tdm_license_1.1,journal-article,19,2,256-263,"Hideyo Shimono, Yukio Sugino",en
+646,71TAK/KUR,4106365.0,10.1016/S0021-9258(18)61885-X,,['The Reversibility of the Adenylate Cyclase Reaction'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,246,18,5843-5845,"Katsuji Takai, Yoshikazu Kurashina, Chiyo Suzuki, Harumasa Okamoto, Akira Ueki, Osamu Hayaishi",en
+647,71TAN/JOH,4945184.0,10.1128/jb.108.3.1107-1111.1971,,['Equilibrium Constant for Conversion of Pyruvate to Acetyl Phosphate and Formate'],3.1.2020,American Society for Microbiology,https://journals.asm.org/non-commercial-tdm-license,journal-article,108,3,1107-1111,"Nobumasa Tanaka, Marvin J. Johnson",en
+648,71UNK/GOL,5573236.0,10.1016/S0021-9258(18)62300-2,,['Thermodynamic and Kinetic Aspects of the Reaction of γ-Fluoroglutamate with d-Glutamate Cyclase'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,246,8,2354-2359,Jay C. Unkeless,en
+649,71WIL/ROC,5580657.0,10.1021/bi00784a017,,-,-,-,-,-,-,-,-,-,-
+650,71WOH,4398630.0,10.1111/j.1432-1033.1971.tb01503.x,,['Equilibrium of the ATP:Glutamine Synthetase Adenylyltransferase Reaction'],3.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,21,4,575-581,Robert M. Wohlhueter,en
+651,72BAK/JEN,4344229.0,10.1016/S0021-9258(19)44584-5,,"['Purification and Properties of l-erythro-3,5-Diaminohexanoate Dehydrogenase from a Lysine-fermenting Clostridium']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,247,23,7724-7734,"John J. Baker, Ingming Jeng, H. Albert Barker",en
+652,72CAG/FRI,4337852.0,10.1016/S0021-9258(19)45152-1,,['Enzymatic Phosphorylation of Serine'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,247,11,3382-3392,"Lauren M. Cagen, Herbert C. Friedmann",en
+653,72COO/MEI,5059882.0,10.1021/bi00755a001,,-,-,-,-,-,-,-,-,-,-
+654,72DAH/AND,5016652.0,10.1016/S0021-9258(19)45519-1,,['d-Fucose Metabolism in a Pseudomonad'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,247,7,2238-2241,"A. Stephen Dahms, Richard L. Anderson",en
+655,72DEL,4624446.0,10.1016/S0021-9258(19)45108-9,,['The Purification and Properties of Sucrose Synthetase from Etiolated Phaseolus aureus Seedlings'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,247,12,3822-3828,Deborah Pierson Delmer,en
+656,72DUF/NEL,5019592.0,10.1111/j.1471-4159.1972.tb01417.x,,['CEREBRAL CARBOHYDRATE METABOLISM DURING ACUTE HYPOXIA AND RECOVERY1'],5.10.2006,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,19,4,959-977,"T. E. Duffy, S. R. Nelson, O. H. Lowry",en
+657,72FOR/GAU,4335290.0,10.1021/bi00756a026,,-,-,-,-,-,-,-,-,-,-
+658,72GUS/GAN,5012314.0,10.1016/S0021-9258(19)45571-3,,['Uridine Diphosphate Glucose Pyrophosphorylase from Sorghum vulgare'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,247,5,1387-1397,"G.L. Gustafson, J.E. Gander",en
+659,72KHA/ZHE,4660956.0,,,-,-,-,-,-,-,-,-,-,-
+660,72KOR/HUR,,10.1016/0005-2744(72)90965-5,,['Purification and properties of an NADP+-dependent glycerol dehydrogenase from rabbit skeletal muscle'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,258,1,40-55,"Alfred W. Kormann, Robert O. Hurst, T.G. Flynn",en
+661,72LEH/TAN,,10.1016/0076-6879(72)28075-2,,-,-,-,-,-,-,-,-,-,-
+662,72MAR/BEL,4623846.0,10.1016/S0021-9258(19)45234-4,,['Metabolism of Trehalose in Euglena gracilis'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,247,10,3223-3228,"Luis R. Maréchal, Enrique Belocopitow",en
+663,72NAG/JAE,4403556.0,10.1515/bchm2.1972.353.1.773,,-,-,-,-,-,-,-,-,-,-
+664,72NEL/KIE,5082943.0,10.1016/0003-2697(72)90451-4,,['Enthalpy of decomposition of hydrogen peroxide by catalase at 25° C (with molar extinction coefficients of H2O2 solutions in the UV)'],10.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,49,2,474-478,"Dennis P. Nelson, Lutz A. Kiesow",en
+665,72ROS/SLA,,10.1016/0005-2728(72)90116-8,,['The value of ΔG° for the hydrolysis of ATP'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,267,2,275-290,"J. Rosing, E.C. Slater",en
+666,72STU,5061975.0,10.1016/S0021-9258(19)45701-3,,['The Enthalpy of Hydrolysis of Acetylcholine'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,247,3,968-969,Julian M. Sturtevant,en
+667,72TAK/ONO,,10.1093/oxfordjournals.jbchem.a129946,,-,-,-,-,-,-,-,-,-,-
+668,72WOL,,10.1101/SQB.1973.037.01.076,,-,-,-,-,-,-,-,-,-,-
+669,72WUR/HES,,10.1016/0014-5793(72)80311-9,,"[""Glucose‐6‐phosphate‐1‐epimerase from baker's yeast. A new enzyme""]",25.7.2002,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,23,3,341-344,"Bernd Wurster, Benno Hess",en
+670,73BEE/STE,,,,-,-,-,-,-,-,-,-,-,-
+671,73DEW/LOW,4697392.0,10.1016/S0021-9258(19)44082-9,,['Myokinase Equilibrium'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,248,8,2829-2835,"Paul De Weer, Allan G. Lowe",en
+672,73GUY/GEL,4743509.0,10.1016/S0021-9258(19)43346-2,,"['Equilibrium Constants of the Malate Dehydrogenase, Citrate Synthase, Citrate Lyase, and Acetyl Coenzyme A Hydrolysis Reactions under Physiological Conditions']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,248,20,6957-6965,"Robert W. Guynn, Harris J. Gelberg, Richard L. Veech",en
+673,73GUY/VEE,4355193.0,10.1016/S0021-9258(19)43347-4,,['The Equilibrium Constants of the Adenosine Triphosphate Hydrolysis and the Adenosine Triphosphate-Citrate Lyase Reactions'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,248,20,6966-6972,"Robert W. Guynn, Richard L. Veech",en
+674,73HAN/RUD,4270771.0,10.1016/S0021-9258(19)43267-5,,['Rabbit Muscle Phosphofructokinase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,248,22,7852-7859,"Ronald L. Hanson, Frederick B. Rudolph, Henry A. Lardy",en
+675,73HAV/PIT,,10.1007/978-1-4615-8897-9_45,,-,-,-,-,-,-,-,-,-,-
+676,73HER,4745770.0,10.1016/S0021-9258(19)43289-4,,['Malate Adenosine Triphosphate Lyase'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,248,21,7295-7303,Louis B. Hersh,en
+677,73LAN,,10.1007/978-1-4684-6985-1_70,,-,-,-,-,-,-,-,-,-,-
+678,73MCC/KOL,,10.1139/o73-069,,['Temperature-Dependent Transition in L-Histidine Ammonia-Lyase'],18.12.2009,Canadian Science Publishing,http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining,journal-article,51,5,556-559,"Ronald W. McClard, Harold M. Kolenbrander",en
+679,73RAD/HOC,,10.1016/0005-2744(73)90065-X,,['Phosphotransacetylase from Bacillus subtilis: Purification and physiological studies'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,321,1,114-125,"Thomas A. Rado, James A. Hoch",en
+680,73ROT/KIS,4201495.0,10.1016/S0021-9258(19)43266-3,,['Calorimetric Studies of Thymidylate Synthesis'],5.2.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,248,22,7845-7851,"Sara W. Rothman, Roy L. Kisliuk, Neal Langerman",en
+681,73SHE/GUL,,,,-,-,-,-,-,-,-,-,-,-
+682,73SOM/COS,4711468.0,10.1021/bi00738a008,,-,-,-,-,-,-,-,-,-,-
+683,73STU/GER,,10.1021/ja00805a036,,-,-,-,-,-,-,-,-,-,-
+684,73SUG,4719122.0,10.1021/bi00739a014,,-,-,-,-,-,-,-,-,-,-
+685,73SUZ/IWA,,10.1093/oxfordjournals.pcp.a074864,,-,-,-,-,-,-,-,-,-,-
+686,73VEL/GUY,4718747.0,10.1016/S0021-9258(19)43738-1,,['The Concentrations of Free and Bound Magnesium in Rat Tissues'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,248,13,4811-4819,"Dulce Veloso, Robert W. Guynn, Marianne Oskarsson, Richard L. Veech",en
+687,73VID/UDE,,10.1016/0005-2744(73)90337-9,,['Inositol dehydrogenase from the yeast Crytococcus melibiosum'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,293,2,295-303,"M. Vidal-Leiria, N. Van Uden",en
+688,73WUR/HES,4279207.0,10.1515/bchm2.1973.354.1.407,,-,-,-,-,-,-,-,-,-,-
+689,74BEL/MAR,4212162.0,10.1111/j.1432-1033.1974.tb03659.x,,['Metabolism of Trehalose in Euglena gracilis'],4.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,46,3,631-637,"Enrique BELOCOPITOW, Luis R. MARÉCHAL",en
+690,74BOS/YAM,4826883.0,10.1021/bi00707a008,,-,-,-,-,-,-,-,-,-,-
+691,74BUR,4156827.0,10.1042/bj1430365,,-,-,-,-,-,-,-,-,-,-
+692,74CHE/PAT,,10.1016/0020-711X(74)90096-2,,"[""Cyclic 3', 5'-nucleotide phosphodiesterase. The extent of reversibility of the reaction and the enthalpy of hydrolysis of cyclic AMP""]",12.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,5,3,311-319,"Wai Yiu Cheung, Sandra M. Patrick, Sam N. Pennington",en
+693,74CLA/BIR,4854821.0,10.1042/bj1390491,,-,-,-,-,-,-,-,-,-,-
+694,74DAN/CAR,4548670.0,10.1111/j.1432-1033.1974.tb03763.x,,['Deoxyribosyl Transfer Catalysis with trans‐N‐Deoxyribosylase'],3.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,48,1,255-262,"Charles DANZIN, Robert CARDINAUD",en
+695,74FER/STR,4219834.0,10.1042/bj1440477,,-,-,-,-,-,-,-,-,-,-
+696,74FLO/FLE,,10.1016/S0021-9258(19)42596-9,,"['Thermodynamic Parameters for the Hydrolysis of Inorganic Pyrophosphate at pH 7.4 as a Function of [Mg2+], [K+], and Ionic Strength Determined from Equilibrium Studies of the Reaction']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,249,11,3465-3474,"Hans Flodgaard, Peter Fleron",en
+697,74FRA/LEE,,,,-,-,-,-,-,-,-,-,-,-
+698,74GAU/MAI,4150793.0,10.1016/S0021-9258(19)42739-7,,['Uridine Diphosphate Galacturonate 4-Epimerase from the Blue-Green Alga Anabaena flos-aquae'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,249,8,2366-2372,"Mary A. Gaunt, Utpalendu S. Maitra, Helmut Ankel",en
+699,74GUY/VEL,4374936.0,10.1042/bj1400369,,-,-,-,-,-,-,-,-,-,-
+700,74GUY/WEB,4275341.0,10.1016/S0021-9258(19)42664-1,,['Equilibrium Constants of the Reactions of Acetyl Coenzyme A Synthetase and the Hydrolysis of Adenosine Triphosphate to Adenosine Monophosphate and Inorganic Pyrophosphate'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,249,10,3248-3254,"Robert W. Guynn, Leslie T. Webster, Richard L. Veech",en
+701,74JEB/TY,4373722.0,10.1073/pnas.71.11.4630,,-,-,-,-,-,-,-,-,-,-
+702,74KEN,4831620.0,,,-,-,-,-,-,-,-,-,-,-
+703,74KNA/BLA,4615902.0,10.1111/j.1432-1033.1974.tb03894.x,,['Pyruvate Formate‐Lyase of Escherichia coli: the Acetyl‐Enzyme Intermediate'],3.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,50,1,253-263,"Joachim KNAPPE, Hans P. BLASCHKOWSKI, Peter GRÖBNER, Thomas SCHMTTT",en
+704,74KUR/TAK,4846750.0,10.1016/S0021-9258(19)42395-8,,['Adenylate Cyclase from Brevibacterium liquefaciens'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,249,15,4824-4828,"Yoshikazu Kurashina, Katsuji Takai, Chiyo Suzuki-Hori, Harumasa Okamoto, Osamu Hayaishi",en
+705,74LAN,,,,-,-,-,-,-,-,-,-,-,-
+706,74MCG/PHI,4364415.0,10.1016/S0021-9258(19)42648-3,,['Purification and Kinetic Characterization of a Monovalent Cation-activated Glycerol Dehydrogenase from Aerobacter aerogenes'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,249,10,3132-3139,"W. Glenn McGregor, James Phillips, Clarence H. Suelter",en
+707,74MCK,,,,-,-,-,-,-,-,-,-,-,-
+708,74SCA/SHI,,10.1002/star.19740261202,,['Studies in the Isomerization of d‐Glucose'],4.11.2006,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,26,12,405-408,"B. L. Scallet, K. Shieh, I. Ehrenthal, L. Slapshak",en
+709,74SCH/STU,,,,-,-,-,-,-,-,-,-,-,-
+710,74TUR/GIL,4436332.0,10.1016/S0021-9258(19)81292-9,,['Uridine Diphosphate Glucose Pyrophosphorylase'],7.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,249,23,7695-7700,"Richard L. Turnquist, Tedford A. Gillett, R.G. Hansen",en
+711,74UEB/BLA,4217278.0,10.1111/j.1432-1033.1974.tb03780.x,,"['Reaction Mechanism of d-Galactose Dehydrogenases from Pseudomonas saccharophila and Pseudomonas fluorescens. Formation and Rearrangement of Aldono-1,5-lactones']",3.3.2005,Wiley,http://doi.wiley.com/10.1002/tdm_license_1.1,journal-article,48,2,389-405,"Karl-Heinz UEBERSCHAR, Ernst-Otto BLACHNITZKY, Gerhart KURZ",en
+712,74WON/FRE,4606575.0,10.1021/bi00716a011,,-,-,-,-,-,-,-,-,-,-
+713,75BOH/SCH,241184.0,,,-,-,-,-,-,-,-,-,-,-
+714,75BRA/JAR,1117007.0,10.1016/S0021-9258(19)41718-3,,['Studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Purification and partial characterization.'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,250,6,2315-2318,"SS Braithwaite, J Jarabak",en
+715,75COH/LYN,,10.1016/0005-2744(75)90324-1,,['Catalytic and thermodynamic properties of the urocanate hydratase reaction'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,377,2,444-453,"Murray S. Cohn, Marjorie C. Lynch, Allen T. Phillips",en
+716,75DON/BAR,,10.1016/0040-6031(75)80018-9,,['Thermochemistry of the reaction catalyzed by lactate dehydrogenase'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,11,2,151-156,"Larry Donnovan, Kathryn Barclay, Kenneth Otto, Neil Jespersen",en
+717,75GER/WES,168198.0,10.1016/S0021-9258(19)41278-7,,"['The enthalpies of hydrolysis of acyclic, monocyclic, and glycoside cyclic phosphate diesters.']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,250,13,5059-5067,"J A Gerlt, F H Westheimer, J M Sturtevant",en
+718,75GOL,240453.0,10.1016/0301-4622(75)80011-1,,['Thermodynamics of hexokinase-catalyzed reactions'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,3,3,192-205,Robert N. Goldberg,en
+719,75GOR/ESF,237482.0,10.1016/0003-9861(75)90274-x,,['Glutathione: Its reaction with NADP and its oxidation-reduction potential'],10.2.2005,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,168,2,450-454,"George Gorin, Ayoub Esfandi, G.B. Guthrie",en
+720,75GRI/CAR,,10.1016/0076-6879(75)42149-8,,-,-,-,-,-,-,-,-,-,-
+721,75IZU/REE,240851.0,10.1016/S0021-9258(19)40819-3,,"['Purification, crystallization, and properties of D-ribose isomerase from Mycobacterium smegmatis.']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,250,20,8085-8087,"K Izumori, AW Rees, AD Elbein",en
+722,75JEN/NYG,235429.0,10.1111/j.1432-1033.1975.tb03925.x,,['Purine Nucleoside Phosphorylase from Escherichia coli and Salmonella typhimurium'],3.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,51,1,253-265,"Kaj Frank JENSEN, Per NYGAARD",en
+723,75JES,1133398.0,10.1021/ja00840a006,,-,-,-,-,-,-,-,-,-,-
+724,75KAP/BAR,,,,-,-,-,-,-,-,-,-,-,-
+725,75KRI,,10.1016/S0076-6879(75)41094-1,,-,-,-,-,-,-,-,-,-,-
+726,75KUR/KON,,,,-,-,-,-,-,-,-,-,-,-
+727,75MAN/LAN,808172.0,10.1016/0003-9861(75)90324-0,,['The enthalpy of oxidation of flavin mononucleotide'],10.2.2005,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,169,1,126-133,"Andrew Mangold, Neal Langerman",en
+728,75MCC/JOV,1092683.0,10.1016/S0021-9258(19)41388-4,,['The steady state kinetic parameters and non-processivity of Escherichia coli deoxyribonucleic acid polymerase I'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,250,11,4073-4080,"WR McClure, TM Jovin",en
+729,75MCG/JOR,,10.1021/ac60356a048,,-,-,-,-,-,-,-,-,-,-
+730,75MUR/TSU,,10.1016/0005-2744(75)90040-6,,['Crystallization and some properties of purine nucleoside phosphorylase from chicken liver'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,384,2,390-398,"Koji Murakami, Keizo Tsushima",en
+731,75PIE/GUY,237900.0,10.1016/S0021-9258(19)41323-9,,"['Equilibrium constants of the reactions of choline acetyltransferase, carnitine acetyltransferase, and acetylcholinesterase under physiological conditions.']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,250,12,4445-4450,"J R Pieklik, R W Guynn",en
+732,75SCH/GRE,170102.0,10.1111/j.1432-1033.1975.tb02227.x,,['Prostaglandin 15‐Hydroxy Dehydrogenase from Human Placenta'],3.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,56,1,245-252,"Werner SCHLEGEL, Roy O. GREEP",en
+733,75SCH/RIF,1191642.0,10.1021/bi00695a020,,-,-,-,-,-,-,-,-,-,-
+734,75SHI/BEA,169260.0,10.1016/S0021-9258(19)41016-8,,"[""Reversibility of adenosine 3':5'-monophosphate-dependent protein kinase reactions.""]",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,250,17,6891-6896,"Y Shizuta, J A Beavo, P J Bechtel, F Hofmann, E G Krebs",en
+735,75SUN,241749.0,10.1016/S0021-9258(19)40710-2,,['Ethanolaminephosphate cytidylyltransferase. Purification and characterization of the enzyme from rat liver.'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,250,22,8585-8590,R Sundler,en
+736,75WYR/GRI,1250.0,10.1111/j.1432-1033.1975.tb02418.x,,['Purification and Properties of Isoenzymes of Cinnamyl-Alcohol Dehydrogenase from Soybean-Cell-Suspension Cultures'],3.3.2005,Wiley,http://doi.wiley.com/10.1002/tdm_license_1.1,journal-article,59,1,9-15,"Dorothea WYRAMBIK, Hans GRISEBACH",en
+737,76BER/KLY,7996.0,,,-,-,-,-,-,-,-,-,-,-
+738,76CRA/WAI,182134.0,10.1042/bj1550679,,-,-,-,-,-,-,-,-,-,-
+739,76FAR/CRY,819440.0,10.1016/S0021-9258(17)33309-4,,['Adenosine triphosphate sulfurylase from penicillium chrysogenum. Steady state kinetics of the forward and reverse reactions.'],4.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,251,14,4389-4397,"J R Farley, D F Cryns, Y H Yang, I H Segel",en
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+741,76GRE/BRI,186026.0,10.1042/bj1570591,,-,-,-,-,-,-,-,-,-,-
+742,76GUY,186456.0,10.1016/S0021-9258(17)32957-5,,['Equilibrium constants under physiological conditions for the reactions of choline kinase and the hydrolysis of phosphorylcholine to choline and inorganic phosphate.'],4.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,251,22,7162-7167,R W Guynn,en
+743,76HIL/ATT,10346.0,10.1099/00221287-96-1-185,,-,-,-,-,-,-,-,-,-,-
+744,76JES,,10.1016/0040-6031(76)80042-1,,['Thermochemistry of the reaction catalyzed by malate dehydrogenase'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,17,1,23-27,Neil Jespersen,en
+745,76LAW/GUY,,,,-,-,-,-,-,-,-,-,-,-
+746,76LLO/KHA,,,,-,-,-,-,-,-,-,-,-,-
+747,76MUR,,10.1093/oxfordjournals.pcp.a075374,,-,-,-,-,-,-,-,-,-,-
+748,76RAO/BUT,186451.0,10.1016/S0021-9258(17)32930-7,,['31P NMR studies of the arginine kinase reaction. Equilibrium constants and exchange rates at stoichiometric enzyme concentration.'],4.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,251,22,6981-6986,"B D Rao, D H Buttlaire, M Cohn",en
+749,76RUS/MUL,12947.0,10.1111/j.1432-1033.1976.tb11021.x,,['CO2 Reduction to Formate by NADH Catalysed by Formate Dehydrogenase from Pseudomonas oxalaticus'],3.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,70,2,325-330,"Ulrich RUSCHING, Ulrich MÜLLER, Peter WILLNOW, Thomas HÖPNER",en
+750,76SCH/KRI,,10.1016/0005-2744(76)90051-6,,['Microcalorimetric methods for substrate determination in flow systems with immobilized enzymes'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,429,1,283-290,"H.-L. Schmidt, G. Krisam, G. Grenner",en
+751,76SPR/LIM,1276393.0,10.1002/bit.260180504,,['A model for enzymatic isomerization of D‐glucose to D‐fructose in a batch reactor'],29.12.2004,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,18,5,633-648,"Robert D. Sproull, Henry C. Lim, Daniel R. Schneider",en
+752,76TRI/PAR,1259718.0,10.1042/bj1530089,,-,-,-,-,-,-,-,-,-,-
+753,76WEI/KIR,949971.0,10.1111/j.1432-1033.1976.tb10350.x,,['The Mechanism of the Synthesis of Indoleglycerol Phosphate Catalyzed by Tryptophan Synthase from Escherichia coli'],3.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,65,2,365-373,"Wolf gang O. WEISCHET, Kasper KIRSCHNER",en
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+755,77ANT/GIN,36553.0,,,-,-,-,-,-,-,-,-,-,-
+756,77APP/NAI,201249.0,10.1042/bj1670087,,-,-,-,-,-,-,-,-,-,-
+757,77GRI/LOC,,10.1016/S0003-2670(01)93665-7,,['The enthalpimetric determination of the michaelis constant of the α-chymotrypsin-catalysed hydrolysis of n-acetyl-l-tyrosine ethyl ester based on the integrated michaelis—menten equation'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,91,2,243-250,"J.K. Grime, K. Lockhart, B. Tan",en
+758,77LAN/GAR,,10.1002/aic.690230102,,['Enzymatic regeneration of ATP: II. Equilibrium studies with acetate kinase and adenylate kinase'],23.6.2004,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,23,1,1-10,"Robert S. Langer, Colin R. Gardner, Bruce K. Hamilton, Clark K. Colton",en
+759,77REH/JAN,,10.1093/clinchem/23.2.195,,['Calorimetric enzymic measurement of uric acid in serum.'],20.1.2020,Oxford University Press (OUP),https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model,journal-article,23,2,195-199,"N N Rehak, G Janes, D S Young",en
+760,77SCH/CLE,836801.0,10.1021/bi00623a001,,-,-,-,-,-,-,-,-,-,-
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+762,77SRA/FRE,18103.0,10.1016/0003-9861(77)90496-9,,['Steady state kinetic mechanism of the Escherichia coli coenzyme A transferase'],10.2.2005,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,181,1,178-184,"Stephen J. Sramek, Frank E. Frerman",en
+763,77TRA/JON,925000.0,10.1016/S0021-9258(19)75229-6,,"[""Kinetic and conformational studies of the orotate phosphoribosyltransferase:orotidine-5'-phosphate decarboxylase enzyme complex from mouse Ehrlich ascites cells""]",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,252,23,8374-8381,"T.W. Traut, M.E. Jones",en
+764,77VEE/KRU,,10.1515/9783110853704-023,,-,-,-,-,-,-,-,-,-,-
+765,78CHR/MAT,30336.0,10.1016/0003-2697(78)90745-5,,['Radloassay of dihydroorotase utilizing ion-exchange chromatography'],7.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,89,1,225-234,"Richard I. Christopherson, Takao Matsuura, Mary Ellen Jones",en
+766,78ERB/BUR,28770.0,10.1016/0005-2744(78)90198-5,,['The kinetics of methyl viologen oxidation and reduction by the hydrogenase from Clostridium pasteurianium'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,525,1,45-54,"David L. Erbes, R.H. Burris",en
+767,78INF/KIN,,10.1016/0005-2744(78)90135-3,,['A novel method for determining equilibrium constants. CTP:phosphorylcholine cytidyltransferase'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,526,2,440-449,"Juan P. Infante, John E. Kinsella",en
+768,78LYN/GUY,204656.0,10.1016/S0021-9258(17)40856-8,,['Equilibrium constants under physiological conditions for the reactions of succinyl coenzyme A synthetase and the hydrolysis of succinyl coenzyme A to coenzyme A and succinate.'],4.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,253,8,2546-2553,"R. Lynn, R.W. Guynn",en
+769,78MCG/BRO,,10.1016/0005-2760(78)90010-3,,['Cholesterol oxidase: Thermochemical studies and the influence of hydroorganic solvents on enzyme activity'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,530,2,247-257,"E.T. McGuinness, H.D. Brown, S.K. Chattopadhyay, F. Chen",en
+770,78MEE/AKE,639798.0,10.1111/j.1432-1033.1978.tb12183.x,,['Relationship between Oxygen Uptake of Perifused Rat-Liver Cells and the Cytosolic Phosphorylation State Calculated from Indicator Metabolites and a Redetermined Equilibrium Constant'],3.3.2005,Wiley,http://doi.wiley.com/10.1002/tdm_license_1.1,journal-article,84,2,421-428,"Roelof MEER, Theodorus P. M. AKERBOOM, Albert K. GROEN, Joseph M. TAGER",en
+771,78OKA/GEN,,10.5458/jag1972.25.113,,-,-,-,-,-,-,-,-,-,-
+772,78RAO/COH,203583.0,10.1016/S0021-9258(17)38123-1,,"['Differentiation of nucleotide binding sites and role of metal ion in the adenylate kinase reaction by 31P NMR. Equilibria, interconversion rates, and NMR parameters of bound substrates']",4.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,253,4,1149-1158,"B.D. Nageswara Rao, M. Cohn, L. Noda",en
+773,78ROS/DUB,213437.0,10.1016/S0021-9258(17)34332-6,,['Phosphoglycerate mutase. Kinetics and effects of salts on the mutase and bisphosphoglycerate phosphatase activities of the enzyme from chicken breast muscle.'],18.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,253,23,8583-8592,"Z.B. Rose, S. Dube",en
+774,78SUB,623877.0,10.1016/0301-4622(78)85013-3,,['Thermodynamics of the glutamate dehydrogenase catalytic reaction'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,7,4,375-378,S. Subramaniun,en
+775,79BYE/SHE,375973.0,10.1021/bi00579a006,,-,-,-,-,-,-,-,-,-,-
+776,79COR/CRO,,,,-,-,-,-,-,-,-,-,-,-
+777,79COR/LEA,447732.0,10.1016/S0021-9258(18)50399-9,,['Effects of free magnesium concentration and ionic strength on equilibrium constants for the glyceraldehyde phosphate dehydrogenase and phosphoglycerate kinase reactions.'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,254,14,6522-6527,"N W Cornell, M Leadbetter, R L Veech",en
+778,79FLE/TAT,,10.1007/BF01732029,,['Energetics of peptide bond formation at elevated temperatures'],13.6.2005,Springer Science and Business Media LLC,http://www.springer.com/tdm,journal-article,12,4,349-355,"A. W. Flegmann, R. Tattersall",en
+779,79GRI/TAN,,10.1016/S0003-2670(01)93222-2,,-,-,-,-,-,-,-,-,-,-
+780,79KIM/PET,475389.0,10.1016/0003-9861(79)90327-8,,"['Malate dehydrogenase. Kinetic studies with meso-tartrate and 2-keto-3-hydroxysuccinate, comparison of the mitochondrial and supernatant pig heart enzymes']",10.2.2005,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,195,1,66-73,"Douglas F. Kimball, Larry Peterson, Daniel J. Mcloughlin, Raymond G. Wolfe",en
+781,79LAB/DEB,231463.0,10.1016/S0300-9084(80)80264-1,,"[""Étude de l'hydrolyse enzymatique d'un ester phosphonique par microcalorimétrie""]",31.5.2007,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,61,9,1091-1094,"Michel Labadie, Jean Debord, Jean-Christian Breton",fr
+782,79LAW/VEE,36398.0,10.1016/S0021-9258(18)50400-2,,['Effects of pH and free Mg2+ on the Keq of the creatine kinase reaction and other phosphate hydrolyses and phosphate transfer reactions.'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,254,14,6528-6537,"J W Lawson, R L Veech",en
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+784,79PIR/LIL,527937.0,10.1515/bchm2.1979.360.2.1693,,-,-,-,-,-,-,-,-,-,-
+785,79RAO/KAY,429312.0,10.1016/S0021-9258(17)30127-8,,"['31P NMR studies of enzyme-bound substrates of rabbit muscle pyruvate kinase. Equilibrium constants, exchange rates, and NMR parameters.']",18.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,254,8,2689-2696,"B.D. Nageswara Rao, F.J. Kayne, M. Cohn",en
+786,79REK/EGO,,,,-,-,-,-,-,-,-,-,-,-
+787,79SCH/HIN,500017.0,10.1515/bchm2.1979.360.2.1497,,-,-,-,-,-,-,-,-,-,-
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+789,79VAN/DEB,376783.0,10.1111/j.1471-4159.1979.tb02290.x,,['DT‐n‐PROPYLACETATE AND GABA DEGRADATION. PREFERENTIAL INHIBITION OF SUCCINIC SEMIALDEHYDE DEHYDROGENASE AND INDIRECT INHIBITION OF GABA‐TRANSAMINASE'],5.10.2006,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,32,6,1769-1780,"J. W. Van Der Laan, Th. De Boer, J. Brunivels",en
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+792,80CAM/SGA,6778396.0,10.1016/0003-9861(80)90098-3,,['The standard gibbs free energy change of hydrolysis of α-d-ribose 1-phosphate'],10.2.2005,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,205,1,191-197,"Marcella Camici, Francesco Sgarrella, Pier L. Ipata, Umberto Mura",en
+793,80CHE/HED,7437498.0,10.1016/0301-4622(80)80041-x,,['A microcalorimetric study of the reaction catalysed by pyruvate kinase'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,12,1,73-82,"Raewyn L. Cheer, Gavin R. Hedwig, Ian D. Watson",en
+794,80COO/BLA,7000186.0,10.1021/bi00562a023,,-,-,-,-,-,-,-,-,-,-
+795,80ELM/HAS,6243283.0,10.1016/S0021-9258(19)86229-4,,['Studies on the phosphorylation and dephosphorylation of L-type pyruvate kinase by the catalytic subunit of cyclic AMP-dependent protein kinase.'],7.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,255,2,668-675,"M.R. El-Maghrabi, W.S. Haston, D.A. Flockhart, T.H. Claus, S.J. Pilkis",en
+796,80FUK/OBO,6987227.0,10.1016/S0021-9258(19)85794-0,,['The enzymes of the galactose cluster in Saccharomyces cerevisiae. II. Purification and characterization of uridine diphosphoglucose 4-epimerase.'],7.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,255,7,2705-2707,"T. Fukasawa, K. Obonai, T. Segawa, Y. Nogi",en
+797,80GER/GUT,,10.1021/ja00525a033,,-,-,-,-,-,-,-,-,-,-
+798,80JAF/COH,6988421.0,10.1016/S0021-9258(19)85684-3,,"[""Shift of the equilibrium constant of the 3-P-glycerate kinase reaction towards 1,3-bis-P-glycerate with adenosine 5'-O-(2-thiotriphosphate) (ATP beta S) as substrate.""]",7.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,255,8,3240-3241,"E.K. Jaffe, M. Cohn",en
+799,80LER/COH,6997302.0,10.1016/S0021-9258(18)43565-X,,"['31P NMR quantitation of the displacement of equilibria of arginine, creatine, pyruvate, and 3-P-glycerate kinase reactions by substitution of sulfur for oxygen in the beta phosphate of ATP.']",5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,255,18,8756-8760,"C.L. Lerman, M. Cohn",en
+800,80PET/AMI,,10.1016/0305-0491(80)90077-2,,['Regulation of glutamate oxidation in mitochondria of Xenopus laevis oocytes'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,66,1,1-11,"Delio Petrucci, Fernanda Amicarelli, Bruno Paponetti, Anna M. Ragnelli",en
+801,80REK/EGO,,,,-,-,-,-,-,-,-,-,-,-
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+803,80SVE/GAL,,,,-,-,-,-,-,-,-,-,-,-
+804,80SVE/MAR,,10.1016/0141-0229(80)90070-8,,['Enzymatic synthesis of β-lactam antibiotics: A thermodynamic background'],28.12.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,2,2,138-144,"Vytas K. Švedas, Alexei L. Margolin, Ilya V. Berezin",en
+805,80TER/RAB,7388069.0,,,-,-,-,-,-,-,-,-,-,-
+806,81GON/CHE,16345717.0,10.1128/aem.41.2.430-436.1981,,['Production of Ethanol from\n d\n -Xylose by Using\n d\n -Xylose Isomerase and Yeasts'],1.1.2020,American Society for Microbiology,https://journals.asm.org/non-commercial-tdm-license,journal-article,41,2,430-436,"Cheng-Shung Gong, Li-Fu Chen, Michael C. Flickinger, Lin-Chang Chiang, George T. Tsao",en
+807,81GRI/CLE,6794611.0,10.1021/bi00523a002,,-,-,-,-,-,-,-,-,-,-
+808,81HIN/POL,6272654.0,10.1016/0003-9861(81)90344-1,,['The enthalpy changes upon hydrolysis of guanosine triphosphate anhydride and ester bonds'],14.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,212,1,72-77,"Hans-Jürgen Hinz, Peter Pollwein, Renate Schmidt, Franz Zimmermann",en
+809,81HIR,16661650.0,10.1104/pp.67.2.221,,['Purification and Characteristics of Sorbitol-6-phosphate Dehydrogenase from Loquat Leaves'],13.12.2008,Oxford University Press (OUP),http://aspb.org/publications/aspb-journals/open-articles,journal-article,67,2,221-224,Masashi Hirai,en
+810,81HSI/SU,,,,-,-,-,-,-,-,-,-,-,-
+811,81KIS/NIE,7030216.0,10.1016/0003-9861(81)90496-3,,['Purification and kinetic characterization of mannitol-1-phosphate dehydrogenase from Aspergillus niger'],10.2.2005,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,211,2,613-621,"Randall C. Kiser, Walter G. Niehaus",en
+812,81MER/MCA,7198894.0,10.1016/0003-9861(81)90416-1,,['Equilibrium constants under physiological conditions for the reactions of d-3-phosphoglycerate dehydrogenase and l-phosphoserine aminotransferase'],14.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,212,2,717-729,"David K. Merrill, Joseph C. McAlexander, Robert W. Guynn",en
+813,81PAH/JAG,,10.1016/S0044-328X(81)80048-7,,['Thermodynamische Betrachtungen über die reversible Reaktionssequenz Glutaminsaure ⇌ Prolin'],19.12.2013,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,101,2,137-144,"E. Pahlich, H.-J. Jäger, E. Kaschel",en
+814,81RAM/PIC,,10.1139/m81-164,,['AMP metabolism by the marine bacterium Vibrio (Beneckea) natriegens: purification and properties of adenylate kinase'],20.5.2010,Canadian Science Publishing,http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining,journal-article,27,10,1053-1059,"Karamchand Ramotar, Michael A. Pickard",en
+815,81RAO/COH,7462219.0,10.1016/S0021-9258(19)69866-2,,"['31P NMR of enzyme-bound substrates of rabbit muscle creatine kinase. Equilibrium constants, interconversion rates, and NMR parameters of enzyme-bound complexes.']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,256,4,1716-1721,"B.D. Nageswara Rao, M. Cohn",en
+816,81SUG/VEI,7197134.0,,,-,-,-,-,-,-,-,-,-,-
+817,82BAR/HEB,,10.1016/0076-6879(82)83045-0,,-,-,-,-,-,-,-,-,-,-
+818,82DEM,,10.1111/j.1749-6632.1982.tb25773.x,,['MECHANISM OF ATP SYNTHESIS BY SARCOPLASMIC RETICULUM ATPase*'],17.12.2006,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,402,1,535-548,Leopoldo de Meis,en
+819,82GAL/SVE,,10.1016/0167-4838(82)90242-4,,['A kinetic study of hog kidney aminoacylase'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,701,3,389-394,"Igor Yu. Galaev, Vytas K. s̆vedas",en
+820,82GUY,6293382.0,10.1016/0003-9861(82)90315-0,,['Equilibrium constants under physiological conditions for the reactions of the nonphosphorylated pathway of l-serine biosynthesis'],10.2.2005,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,218,1,14-25,Robert W. Guynn,en
+821,82GUY/THA,6284052.0,10.1016/0003-9861(82)90110-2,,['Equilibrium constants under physiological conditions for the reactions of l-phosphoserine phosphatase and pyrophosphate: l-serine phosphotransferase'],14.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,215,2,514-523,"Robert W. Guynn, Howard Thames",en
+822,82HSI/CHI,,10.1016/0141-0229(82)90006-0,,['Effects of borate on isomerization and yeast fermentation of high xylulose solution and acid hydrolysate of hemicellulose'],28.12.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,4,1,25-31,"Humg-Yu Hsiao, Lin-Chang Chiang, Li-Fu Chen, George T. Tsao",en
+823,82NG/WON,7076619.0,10.1128/JB.150.3.1252-1258.1982,,['Properties of oxaloacetate decarboxylase from Veillonella parvula'],3.1.2020,American Society for Microbiology,https://journals.asm.org/non-commercial-tdm-license,journal-article,150,3,1252-1258,"S K Ng, M Wong, I R Hamilton",en
+824,82RED,,,,-,-,-,-,-,-,-,-,-,-
+825,82REH/YOU,,10.1093/clinchem/28.11.2235,,['Enzymic determination of free and esterified cholesterol in serum by microcalorimetry.'],20.1.2020,Oxford University Press (OUP),https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model,journal-article,28,11,2235-2240,"N N Rehak, D S Young",en
+826,82SAL/GIA,,10.1007/BF01959737,,['Apparent equilibrium constant of the hypoxanthine guanine phosphoribosyltransferase-catalyzed IMP-GMP exchange'],1.8.2005,Springer Science and Business Media LLC,http://www.springer.com/tdm,journal-article,38,10,1196-1197,"C. Salerno, A. Giacomello",en
+827,82SAL/JOR,6812503.0,10.1016/0003-9861(82)90487-8,,['31P NMR studies on purine nucleoside phosphorylases: Determination of the scissile bond and of the equilibrium constant'],10.2.2005,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,217,1,139-143,"Salvatore J. Salamone, Frank Jordan, Rosy R. Jordan",en
+828,82SUE/KAT,,10.1016/0304-4165(82)90178-7,,['Purification and characterization of sepiapterin reductase from rat erythrocytes'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,717,2,265-271,"T. Sueoka, S. Katoh",en
+829,83BRA,,,,-,-,-,-,-,-,-,-,-,-
+830,83CRA/BOS,,10.1016/0003-9861(83)90213-8,,['Steady-state kinetic properties of purified rat liver alcohol dehydrogenase: Application to predicting alcohol elimination rates in vivo'],26.11.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,224,1,299-309,"David W. Crabb, William F. Bosron, Ting-Kai Li",en
+831,83HAA/KAR,18551488.0,10.1002/bit.260250715,,['The kinetics of penicillin‐V deacylation on an immobilized enzyme'],29.12.2004,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,25,7,1873-1895,"P. Haagensen, L. G. Karlsen, J. Petersen, J. Villadsen",en
+832,83HON/HAR,,10.1093/oxfordjournals.pcp.a076514,,-,-,-,-,-,-,-,-,-,-
+833,83KAT/SUE,6370350.0,,,-,-,-,-,-,-,-,-,-,-
+834,83KHO/KAR,,,,-,-,-,-,-,-,-,-,-,-
+835,83MIL/RYC,6852021.0,10.1111/j.1432-1033.1983.tb07443.x,,['The αβ‐Methylene Analogues of ADP and ATP Act as Substrates for Creatine Kinase'],3.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,133,1,169-172,"E. James MILNER‐WHITE, David S. RYCROFT",en
+836,83PIL/HAN,6885800.0,10.1016/S0021-9258(17)44524-8,,['Co-purification and characterization of UDP-glucose 4-epimerase and UDP-N-acetylglucosamine 4-epimerase from porcine submaxillary glands.'],4.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,258,17,10774-10778,"F Piller, M H Hanlon, R L Hill",en
+837,83SEL/MAN,6863314.0,10.1016/S0021-9258(18)32137-9,,['Reversal of the reaction catalyzed by glyoxalase I. Calculation of the equilibrium constant for the enzymatic reaction.'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,258,14,8872-8875,"S Sellin, B Mannervik",en
+838,83TIL,,,,-,-,-,-,-,-,-,-,-,-
+839,83VIT/HUA,6357095.0,10.1016/0003-9861(83)90339-9,,['Uridine phosphorylase from Escherichia coli B.: Kinetic studies on the mechanism of catalysis'],14.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,226,2,687-692,"Alberto Vita, Charles Y. Huang, Guilio Magni",en
+840,83WED/BLA,16663114.0,10.1104/pp.72.4.1021,,['Physical and Kinetic Properties and Regulation of the NAD Malic Enzyme Purified from Leaves of Crassula argentea'],13.12.2008,Oxford University Press (OUP),http://aspb.org/publications/aspb-journals/open-articles,journal-article,72,4,1021-1028,"R. T. Wedding, M. Kay Black",en
+841,83YAM/SAI,6822536.0,10.1016/S0021-9258(18)33062-X,,"['Purification and properties of NADP-dependent formate dehydrogenase from Clostridium thermoaceticum, a tungsten-selenium-iron protein.']",5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,258,3,1826-1832,"I Yamamoto, T Saiki, S M Liu, L G Ljungdahl",en
+842,84ADA/UED,18551697.0,10.1002/bit.260260203,,['Kinetics of formation of maltose and isomaltose through condensation of glucose by glucoamylase'],30.12.2004,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,26,2,121-127,"Shuji Adachi, Yasuo Ueda, Kenji Hashimoto",en
+843,84BER/COO,6091737.0,10.1021/bi00313a014,,-,-,-,-,-,-,-,-,-,-
+844,84BLA/COC,6433972.0,10.1021/bi00306a009,,-,-,-,-,-,-,-,-,-,-
+845,84DEM,,10.1016/S0021-9258(20)82109-7,,"['Pyrophosphate of high and low energy. Contributions of pH, Ca2+, Mg2+, and water to free energy of hydrolysis.']",7.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,259,10,6090-6097,L de Meis,en
+846,84DEY,,10.1016/S0031-9422(00)85013-X,,['UDP-galactose 4′-epimerase from vicia faba seeds'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,23,4,729-732,Prakash M. Dey,en
+847,84DIT/KUB,,10.1139/m84-214,,['Xylose metabolism in Pachysolen tannophilus: purification and properties of xylose reductase'],20.5.2010,Canadian Science Publishing,http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining,journal-article,30,11,1330-1336,"Günther Ditzelmüller, Christian P. Kubicek, Wilfried Wöhrer, Max Röhr",en
+848,84DIT/KUB2,,10.1111/j.1574-6968.1984.tb01455.x,,-,-,-,-,-,-,-,-,-,-
+849,84KOL/EGG,6489933.0,10.1515/bchm2.1984.365.2.847,,-,-,-,-,-,-,-,-,-,-
+850,84LLO/CHA,,,,-,-,-,-,-,-,-,-,-,-
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+854,84RAG/LJU,6608524.0,10.1016/S0021-9258(17)43122-X,,"['Purification and properties of NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from Acetobacterium woodii.']",4.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,259,6,3499-3503,"S W Ragsdale, L G Ljungdahl",en
+855,84REK/RUM,,10.1016/0040-6031(84)85121-7,,-,-,-,-,-,-,-,-,-,-
+856,84REK/RUM2,,,,-,-,-,-,-,-,-,-,-,-
+857,84TEW/GOL,,10.1007/BF00647222,,['Thermodynamics of the conversion of aqueous glucose to fructose'],29.11.2004,Springer Science and Business Media LLC,http://www.springer.com/tdm,journal-article,13,8,523-547,"Y. B. Tewari, R. N. Goldberg",en
+858,84UCH/TSU,6389524.0,10.1093/oxfordjournals.jbchem.a134863,,-,-,-,-,-,-,-,-,-,-
+859,84WAS/DAU,6391537.0,10.1021/bi00317a015,,-,-,-,-,-,-,-,-,-,-
+860,85ANS/PRI,,10.1042/bst0130362,,-,-,-,-,-,-,-,-,-,-
+861,85BAD/WAL,3921052.0,10.1021/bi00327a010,,-,-,-,-,-,-,-,-,-,-
+862,85BAR,16664543.0,10.1104/pp.79.4.1127,,['The Equilibrium of the Reaction Catalyzed by Sucrose Phosphate Synthase'],13.12.2008,Oxford University Press (OUP),http://aspb.org/publications/aspb-journals/open-articles,journal-article,79,4,1127-1128,George A. Barber,en
+863,85COO/PRA,3966792.0,10.1016/0003-9861(85)90602-2,,['Hepatic microsomal short-chain β-hydroxyacyl-CoA dehydrase distinct from the fatty acid elongation component: Substrate specificity of the membrane-extracted enzyme'],3.11.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,236,1,26-35,"Lynda Cook, M.Renuka Prasad, Robert Vieth, Dominick L. Cinti",en
+864,85DAS/BRO,4092075.0,10.1016/0301-4622(85)80068-5,,['Enthalpy of acetylcholine hydrolysis by acetylcholinesterase'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,23,1-2,105-114,"Y.T. Das, H.D. Brown, S.K. Chattopadhyay",en
+865,85DEM/BEH,3004566.0,10.1021/bi00347a042,,-,-,-,-,-,-,-,-,-,-
+866,85FAG/DEW,3158649.0,10.1016/S0021-9258(18)88949-9,,['Steady state kinetics of ATP synthesis and hydrolysis coupled calcium transport catalyzed by the reconstituted sarcoplasmic reticulum ATPase.'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,260,10,6147-6152,"M H Fagan, T G Dewey",en
+867,85GAJ/GOL,4052575.0,10.1016/0301-4622(85)80042-9,,['Thermodynamics of the conversion of fumarate to l-(−)-malate'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,22,3,187-195,"E. Gajewski, R.N. Goldberg, D.K. Steckler",en
+868,85GEU/MAY,3841060.0,10.1111/j.1432-1033.1985.tb09305.x,,['Steady‐state kinetics of skeletal muscle myosin light chain kinase indicate a strong down regulation by products'],4.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,153,2,327-334,"Ursula GEUSS, Georg W. MAYR, Ludwig M. G. HEILMEYER",en
+869,85HEA/CHU,4066712.0,10.1016/S0021-9258(17)36245-2,,"['A mitochondrial NADP+-dependent reductase related to the 4-aminobutyrate shunt. Purification, characterization, and mechanism.']",18.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,260,30,16361-16366,"W G Hearl, J E Churchich",en
+870,85HER/AIY,4052045.0,10.1042/bj2300043,,-,-,-,-,-,-,-,-,-,-
+871,85LEE/OSU,2997186.0,10.1016/S0021-9258(17)38662-3,,['The interaction of phosphorothioate analogues of ATP with phosphomevalonate kinase. Kinetic and 31P NMR studies.'],4.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,260,26,13909-13915,"C S Lee, W J O'Sullivan",en
+872,85LIE,,,,-,-,-,-,-,-,-,-,-,-
+873,85MAK/KIE,,10.1002/star.19850370706,,['Glucose Isomerase and Its Behaviour under Hydrogenation Conditions'],4.11.2006,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,37,7,232-241,"M. Makkee, A. P. G. Kieboom, H. van Bekkum",en
+874,85REK/SLO,,10.1016/0040-6031(85)85203-5,,-,-,-,-,-,-,-,-,-,-
+875,85SRI/FIS,3994979.0,10.1021/bi00324a012,,-,-,-,-,-,-,-,-,-,-
+876,85TEW/GOL,,10.1007/BF02824308,,['Thermodynamics of the conversion of aqueous glucose to fructose'],31.1.2008,Springer Science and Business Media LLC,http://www.springer.com/tdm,journal-article,11,1,17-24,"Y. B. Tewari, R. N. Goldberg",en
+877,85TEW/GOL2,3931718.0,10.1016/0301-4622(85)80043-0,,"['An investigation of the equilibria between aqueous ribose, ribulose, and arabinose']",25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,22,3,197-204,"Y.B. Tewari, R.N. Goldberg",en
+878,85TEW/STE,17007786.0,10.1016/0301-4622(85)80041-7,,['Thermodynamics of the conversion of aqueous xylose to xylulose'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,22,3,181-185,"Y.B. Tewari, D.K. Steckler, R.N. Goldberg",en
+879,85VAN/SCH,2864395.0,10.1111/j.1471-4159.1985.tb07214.x,,['Succinic Semialdehyde as a Substrate for the Formation of γ‐Aminobutyric Acid'],5.10.2006,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,45,5,1471-1474,"F. J. van Bemmelen, M. J. Schouten, D. Fekkes, J. Bruinvels",en
+880,85WIE/HIN,3933423.0,10.1016/0003-9861(85)90228-0,,['Thermodynamics of the reactions catalyzed by the multifunctional enzyme complex tryptophan synthase'],3.11.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,242,2,440-446,"Heinrich Wiesinger, Hans-Jürgen Hinz",en
+881,86CAS/VEE,3826613.0,10.1016/0003-2697(86)90338-6,,"['The measurement of xylulose 5-phosphate, ribulose 5-phosphate, and combined sedoheptulose 7-phosphate and ribose 5-phosphate in liver tissue']",8.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,159,2,243-248,"Joseph P. Casazza, Richard L. Veech",en
+882,86CAS/VEE2,3079759.0,10.1016/S0021-9258(17)36148-3,,['The interdependence of glycolytic and pentose cycle intermediates in ad libitum fed rats.'],18.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,261,2,690-698,"J P Casazza, R L Veech",en
+883,86DAL/REN,,10.1016/0003-2697(86)90642-1,,"['ATP sulfurylase-dependent assays for inorganic pyrophosphate: Applications to determining the equilibrium constant and reverse direction kinetics of the pyrophosphatase reaction, magnesium binding to orthophosphate, and unknown concentrations of pyrophosphate']",10.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,157,2,385-395,"Lori A. Daley, Franco Renosto, Irwin H. Segel",en
+884,86DEW/EMI,3741845.0,10.1021/bi00362a022,,-,-,-,-,-,-,-,-,-,-
+885,86GAJ/STE,3528161.0,10.1016/S0021-9258(18)67153-4,,"[""Thermodynamics of the hydrolysis of adenosine 5'-triphosphate to adenosine 5'-diphosphate.""]",5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,261,27,12733-12737,"E Gajewski, D K Steckler, R N Goldberg",en
+886,86GOL/GAJ,17007794.0,10.1016/0301-4622(86)85054-2,,['Thermodynamics of the conversion of aqueous l-aspartic acid to fumaric acid and ammonia'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,24,1,13-23,"R.N. Goldberg, E. Gajewski, D.K. Steckler, Y.B. Tewari",en
+887,86GRA/ELL,,10.1016/0167-4889(86)90050-9,,['A saturation transfer phosphorus nuclear magnetic resonance study of arginine phosphokinase in the muscle of a marine mollusc'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,887,2,157-163,"R.A. Graham, W.R. Ellington, C.P. Chih",en
+888,86HUB/HUR,3083779.0,10.1016/0003-9861(86)90487-x,,['Reversion reactions of β-galactosidase (Escherichia coli)'],3.11.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,246,1,411-418,"R.E. Huber, K.L. Hurlburt",en
+889,86KIM/LEE,,,,-,-,-,-,-,-,-,-,-,-
+890,86KON/POL,,10.1515/zna-1986-1203,,['Zur spektroskopischen Analyse von Redoxgleichgewichten am Beispiel NAD(P)H-abhängiger Dehydrogenasen'],4.2.2015,Walter de Gruyter GmbH,http://creativecommons.org/licenses/by-nc-nd/3.0/,journal-article,41,12,1352-1356,"J. Konstanczak, J. Polster",en
+891,86KUP/FER,,10.1016/0167-4838(86)90316-X,,['Muscle adenylate kinase catalyzes adenosine 5′-tetraphosphate synthesis from ATP and ADP'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,869,1,107-111,"V.V. Kupriyanov, J.A. Ferretti, R.S. Balaban",en
+892,86MEI/GAD,,10.1007/BF00694264,,"['The separate function ofd-lactate-, octopine-, and alanopine dehydrogenases in the foot muscle of the jumping cockleCardium tuberculatum during anaerobiosis']",29.11.2004,Springer Science and Business Media LLC,http://www.springer.com/tdm,journal-article,156,6,873-881,"Georg Meinardus-Hager, Gerd G�de",en
+893,86MEY/BRO,,10.1152/ajpcell.1986.250.2.C264,,-,-,-,-,-,-,-,-,-,-
+894,86NAK/KIM,3792308.0,10.1111/j.1432-1033.1986.tb10476.x,,['Kinetics and equilibrium of enzymatic synthesis of peptides in aqueous/organic biphasic systems'],4.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,161,3,541-549,"Kazuhiro NAKANISHI, Yukitaka KIMURA, Ryuichi MATSUNO",en
+895,86OLI/TOI,18555380.0,10.1002/bit.260280508,,['Sugar cane bagasse as a possible source of fermentable carbohydrates. II. Optimization of the xylose isomerase reaction for isomerization of xylose as well as sugar cane bagasse hydrolyzate to xylulose in laboratory‐scale units'],27.5.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,28,5,684-699,"S. P. Olivier, P. J. du Toit",en
+896,86POL/MEN,,,,-,-,-,-,-,-,-,-,-,-
+897,86PRU/TEN,,10.1016/0167-4838(86)90245-1,,['Is thiocyanate peroxidation at equilibrium in vivo?'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,870,3,385-391,"Kenneth M. Pruitt, Jorma Tenovuo, Britta Mansson-Rahemtulla, Paul Harrington, David C. Baldone",en
+898,86RAG/CAR,3091600.0,10.1016/S0021-9258(18)67242-4,,"[""Purification and characterization of 5'-deoxy-5'-methylthioadenosine phosphorylase from human placenta.""]",5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,261,26,12324-12329,"F Della Ragione, M Cartenì-Farina, V Gragnaniello, M I Schettino, V Zappia",en
+899,86REK/SKY,,10.1016/0165-022X(86)90113-2,,['Simple industrial method for determination of activity of asparaginase and some other enzymes'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,12,4,247-249,"M.V. Rekharsky, A.Zh. Skya, S.V. Lopatnev, Yu.B. Slozhenikina, A.M. Egorov, G.L. Galchenko",en
+900,86ROH/ETT,3769932.0,10.1111/j.1432-1033.1986.tb09975.x,,['Catalysis by hog‐kidney aminoacylase does not involve a covalent intermediate'],4.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,160,2,327-332,"Klaus H. RÖHM, Robert L. VAN ETTEN",en
+901,86TEW/GOL,17007802.0,10.1016/0301-4622(86)85034-7,,['Thermodynamics of carbohydrate isomerization reactions'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,24,3,291-294,"Y.B. Tewari, R.N. Goldberg",en
+902,87ANT,,,,-,-,-,-,-,-,-,-,-,-
+903,87BED/TES,3429208.0,,,-,-,-,-,-,-,-,-,-,-
+904,87BUC/MIL,2883006.0,10.1111/j.1432-1033.1987.tb11164.x,,['Equilibrium constants of several reactions involved in the fermentation of glutamate'],4.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,164,3,565-569,"Wolfgang BUCKEL, Stanley L. MILLER",en
+905,87FIE/JOH,3307916.0,10.1021/bi00387a052,,-,-,-,-,-,-,-,-,-,-
+906,87HSU/WED,3322196.0,10.1016/0003-9861(87)90498-X,,['Kinetic mechanism of native Escherichia coli aspartate transcarbamylase'],7.12.2004,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,259,2,316-330,"Yuchiong Hsuanyu, Frederick C. Wedler",en
+907,87KUC/MIZ,3327522.0,10.1021/bi00399a057,,-,-,-,-,-,-,-,-,-,-
+908,87MIL/EST,3597405.0,10.1016/S0021-9258(18)48039-8,,"['Purification and characterization of 2,5-diketo-D-gluconate reductase from Corynebacterium sp.']",5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,262,19,9016-9020,"J V Miller, D A Estell, R A Lazarus",en
+909,87MOS/FRE,3117791.0,10.1016/S0021-9258(18)48103-3,,"['The role of S-adenosylmethionine in the lysine 2,3-aminomutase reaction.']",5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,262,31,14859-14862,"M Moss, P A Frey",en
+910,87OWU/TRE,,10.1016/0040-6031(87)88028-0,,-,-,-,-,-,-,-,-,-,-
+911,87RAO/HAR,2958459.0,10.1016/S0021-9258(18)47906-9,,['Kinetic mechanism of Ascaris suum phosphofructokinase desensitized to allosteric modulation by diethylpyrocarbonate modification.'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,262,29,14074-14079,"G S Rao, B G Harris, P F Cook",en
+912,87REK/EGO,,10.1016/0040-6031(87)88272-2,,['Thermochemistry of hydrolytic enzymatic reactions'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,112,2,151-160,"M.V. Rekharsky, A.M. Egorov, G.L. Gal'chenko",en
+913,87TAV/LEE,,10.1016/0167-4838(87)90136-1,,['31P-NMR study of the orotate phosphoribosyltransferase equilibrium with thiopyrophosphate as substrate'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,913,3,279-284,"Anne Tavares, Choy Soong Lee, William J. O'Sullivan",en
+914,87TEW/GAJ,,10.1021/j100288a028,,-,-,-,-,-,-,-,-,-,-
+915,87WOL/REI,,10.1016/S0006-3495(88)82934-5,,['Molar enthalpy change for hydrolysis of phosphorylcreatine under conditions in muscle cells'],6.1.2009,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,54,1,97-104,"R.C. Woledge, P.J. Reilly",en
+916,88BED/HAD,3384815.0,10.1016/S0021-9258(19)81556-9,,['Purification and characterization of chalcone isomerase from soybeans.'],7.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,263,20,9582-9588,"R A Bednar, J R Hadcock",en
+917,88BEL/BAE,2848810.0,10.1016/S0021-9258(18)37367-8,,['Purification and characterization of phosphatidylinositol kinase from Saccharomyces cerevisiae.'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,263,35,18897-18903,"C J Belunis, M Bae-Lee, M J Kelley, G M Carman",en
+918,88GAU,2844813.0,10.1016/S0021-9258(19)37602-1,,['Mutated forms of phosphoglycerate mutase in yeast affect reversal of metabolic flux. Effect of reversible and irreversible function of an enzyme on pathway reversal.'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,263,30,15400-15406,"N Gautam, N Gautan",en
+919,88GUI/SNE,3076441.0,,,-,-,-,-,-,-,-,-,-,-
+920,88LIM/RAI,3365378.0,10.1021/bi00404a013,,-,-,-,-,-,-,-,-,-,-
+921,88MAC/FEW,3291854.0,10.1042/bj2500743,,-,-,-,-,-,-,-,-,-,-
+922,88TEW/GOL,2839246.0,10.1016/0301-4622(88)85045-2,,['Thermodynamics of the conversion of penicillin G to phenylacetic acid and 6-aminopenicillanic acid'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,29,3,245-252,"Yadu B. Tewari, Robert N. Goldberg",en
+923,88TEW/STE,3346215.0,10.1016/S0021-9258(18)68976-8,,['Thermodynamics of isomerization reactions involving sugar phosphates.'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,263,8,3664-3669,"Y B Tewari, D K Steckler, R N Goldberg",en
+924,88TEW/STE2,3346216.0,10.1016/S0021-9258(18)68977-X,,['Thermodynamics of hydrolysis of sugar phosphates.'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,263,8,3670-3675,"Y B Tewari, D K Steckler, R N Goldberg, W L Gitomer",en
+925,89AIR,,10.3891/acta.chem.scand.43-0386,,-,-,-,-,-,-,-,-,-,-
+926,89BER/MUD,,10.1016/0165-022X(89)90073-0,,['A stopped-flow mixer device for a batch microcalorimeter application to NAD-NADase reaction'],11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,18,2,113-124,"R.L. Berger, C.P. Mudd, T. Clem, T. Kolobow, E. Beile, P.C. Simons, S. Michel, W. McClintock",en
+927,89ELD/DEG,,10.1002/mrm.1910110111,,['31P NMR studies of the thermodynamics and kinetics of the creatine kinase reaction'],5.3.2007,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,11,1,121-126,"H. Eldar, H. Degani",en
+928,89ELL,2543728.0,10.1242/jeb.143.1.177,,['Phosphocreatine Represents a Thermodynamic and Functional Improvement Over Other Muscle Phosphagens'],25.4.2021,The Company of Biologists,http://www.biologists.com/user-licence-1-1/,journal-article,143,1,177-194,W. Ross Ellington,en
+929,89GOL/TEW,2498341.0,10.1016/S0021-9258(18)81743-4,,['A calorimetric and equilibrium investigation of the hydrolysis of lactose'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,264,17,9897-9900,"R N Goldberg, Y B Tewari",en
+930,89GOL/TEW2,2722882.0,10.1016/S0021-9258(18)81744-6,,['Thermodynamics of the hydrolysis of sucrose'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,264,17,9901-9904,"R N Goldberg, Y B Tewari, J C Ahluwalia",en
+931,89HAG/ROS,2537492.0,10.1073/pnas.86.4.1224,,-,-,-,-,-,-,-,-,-,-
+932,89IMA,,10.1093/oxfordjournals.jbchem.a122954,,-,-,-,-,-,-,-,-,-,-
+933,89JEE/SHI,,,,-,-,-,-,-,-,-,-,-,-
+934,89JOH/HED,,10.1016/0141-0229(89)90018-5,,['Studies of the reversed α-mannosidase reaction in high concentrations of mannose'],4.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,11,6,347-352,"Elisabet Johansson, Lars Hedbys, Klaus Mosbach, Per-Olof Larsson, Alf Gunnarsson, Sigfrid Svensson",en
+935,89JUN/JUN,2663076.0,10.1016/0005-2760(89)90232-4,,['Purification and properties of carnitine dehydratase from Escherichia coli — a new enzyme of carnitine metabolization'],7.4.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,1003,3,270-276,"Heinrich Jung, Kirsten Jung, Hans-Peter Kleber",en
+936,89LEH/SIN,2494984.0,10.1042/bj2570355,,-,-,-,-,-,-,-,-,-,-
+937,89LOP/COH,,10.1016/0167-4838(89)90291-4,,['Direct determination of creatine kinase equilibrium constants with creatine or cyclocreatine as substrate'],7.4.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,998,3,317-320,"Patrizia LoPresti, Mildred Cohn",en
+938,89REK/SIK,,,,-,-,-,-,-,-,-,-,-,-
+939,89RIZ/HAR,,10.1016/0922-338X(89)90081-0,,['A kinetic study of the NAD+-xylitol-dehydrogenase from the yeast Pichia stipitis'],12.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,67,1,25-30,"Manfred Rizzi, Katharina Harwart, Ngoc-Anh Bui-Thanh, Hanswerner Dellweg",en
+940,89ROM/DEM,2722769.0,10.1016/S0021-9258(18)83123-4,,['Role of water in the energy of hydrolysis of phosphoanhydride and phosphoester bonds'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,264,14,7869-7873,"P J Romero, L de Meis",en
+941,89SAN/SIN,,10.1007/BF02703521,,['Characterization of cytosolic phosphoglucoisomerase from immature wheat (Triticum aestivum L.) endosperm'],18.9.2007,Springer Science and Business Media LLC,http://www.springer.com/tdm,journal-article,14,1,47-54,"R. S. Sangwan, Randhir Singh",en
+942,89SCH/GIF,2789134.0,10.1111/j.1432-1033.1989.tb14984.x,,['Purification and properties of a polyol dehydrogenase from the phototrophic bacterium Rhodobacter sphaeroides'],4.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,184,1,15-19,"Karl‐Heinz SCHNEIDER, Friedrich GIFFHORN",en
+943,89TEW/GOL,2492994.0,10.1016/S0021-9258(19)84947-5,,['Thermodynamics of hydrolysis of disaccharides'],7.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,264,7,3966-3971,"Y B Tewari, R N Goldberg",en
+944,90BHA/VIN,2271660.0,10.1021/bi00498a009,,-,-,-,-,-,-,-,-,-,-
+945,90KWI/HUA,2157478.0,10.1021/bi00453a019,,-,-,-,-,-,-,-,-,-,-
+946,90LIU,,,,-,-,-,-,-,-,-,-,-,-
+947,90LIU/QUI,2139795.0,10.1021/bi00458a012,,-,-,-,-,-,-,-,-,-,-
+948,90LUN/APR,2140258.0,10.1042/bj2670739,,-,-,-,-,-,-,-,-,-,-
+949,90OCO/BUT,,10.1016/0304-5102(90)85274-L,,['Benzene boronic acid inhibition of vitamin a-bile-salt.stimulated human milk lipase interactions'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,60,2,255-265,"Charmian J. O'Connor, Paul A.G. Butler, Basma M. Yaghi",en
+950,90SAN/SIN,2341161.0,,,-,-,-,-,-,-,-,-,-,-
+951,91AND/KAT,,10.1021/ja00008a073,,-,-,-,-,-,-,-,-,-,-
+952,91GOL/BEL,1873473.0,10.1016/0301-4622(91)85030-t,,['Thermodynamics of hydrolysis of oligosaccharides'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,40,1,69-76,"Robert N. Goldberg, Donna Bell, Yadu B. Tewari, Michael A. McLaughlin",en
+953,91HOR/UEH,,10.1271/bbb1961.55.1071,,-,-,-,-,-,-,-,-,-,-
+954,91HOR/WAT,,10.3109/10242429109000693,,-,-,-,-,-,-,-,-,-,-
+955,91KLE/RAN,,10.1093/jxb/42.4.537,,-,-,-,-,-,-,-,-,-,-
+956,91KNI/SEM,1645186.0,10.1021/bi00234a019,,-,-,-,-,-,-,-,-,-,-
+957,91KRA/GYG,,10.1002/anie.199108271,,['Enzymatic Two‐Step Synthesis of N‐Acetyl‐neuraminic Acid in the Enzyme Membrane Reactor'],31.12.2003,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,30,7,827-828,"Udo Kragl, Daniel Gygax, Oreste Ghisalba, Christian Wandrey",en
+958,91LIU/FRO,1646815.0,10.1016/S0021-9258(18)99024-1,,"['31P nuclear magnetic resonance spectroscopy studies of substrate and product binding to fructose-1,6-bisphosphatase']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,266,18,11774-11778,"F. Liu, H.J. Fromm",en
+959,91MOR/FRE,1653014.0,10.1021/bi00098a030,,-,-,-,-,-,-,-,-,-,-
+960,91PAR/HOR,1939115.0,10.1016/S0021-9258(18)54759-1,,"['Nucleoside hydrolase from Crithidia fasciculata. Metabolic role, purification, specificity, and kinetic mechanism.']",5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,266,31,20658-20665,"D.W. Parkin, B.A. Horenstein, D.R. Abdulah, B. Estupiñán, V.L. Schramm",en
+961,91SCH/GIF,,10.1016/0141-0229(91)90153-2,,"['Sorbitol dehydrogenase from Pseudomonas sp.: Purification, characterization and application to quantitative determination of sorbitol']",28.12.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,13,4,332-337,"Karl-Heinz Schneider, Friedrich Giffhorn",en
+962,91SEM/CLE,1827991.0,10.1021/bi00234a020,,-,-,-,-,-,-,-,-,-,-
+963,91SRI/NAM,1873475.0,10.1016/0301-4622(91)85032-l,,['Thermodynamic parameters for the glutamate dehydrogenase catalyzed α-imino acid—α-amino acid interconversion'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,40,1,81-87,"R. Srinivasan, Parthasarathy Nambi",en
+964,91TEW/GOL,1873472.0,10.1016/0301-4622(91)85029-p,,['Thermodynamics of hydrolysis of disaccharides'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,40,1,59-67,"Yadu B. Tewari, Robert N. Goldberg",en
+965,91WOH/DIE,,10.1007/BF00243458,,-,-,-,-,-,-,-,-,-,-
+966,92BLA/GUI,,10.1002/bit.260400913,,['The equilibrium and kinetics of N‐acetyl‐tryptophan phenylethyl ester synthesis by agarose–chymotrypsin in organic media'],30.12.2004,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,40,9,1092-1096,"Rosa M. Blanco, José M. Guisán, Peter J. Halling",en
+967,92DEM/ATT,,10.1016/S0232-4393(11)80392-6,,['Equilibrium Kinetics of D-Glucose to D-Fructose Isomerization Catalyzed by Glucose Isomerase enzyme from Streptomyces phaeochromogenus'],17.5.2018,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,147,5,297-303,"Mohamed Demerdash, Rasmy M. Attia",en
+968,92ELL/SRI,1540130.0,10.1042/bj2820155,,-,-,-,-,-,-,-,-,-,-
+969,92IBO/OBO,,10.3109/10242429209003660,,-,-,-,-,-,-,-,-,-,-
+970,92KAH/SCH,1527498.0,10.1099/00221287-138-6-1277,,-,-,-,-,-,-,-,-,-,-
+971,92KEL/SCH,1318300.0,10.1016/S0021-9258(19)49761-5,,"['Purification and characterization of actinomycin synthetase I, a 4-methyl-3-hydroxyanthranilic acid-AMP ligase from Streptomyces chrysomallus.']",6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,267,17,11745-11752,"U Keller, W Schlumbohm",en
+972,92KER/KER,,10.1016/0167-4838(92)90131-V,,"['Purification, characterization and preliminary X-ray study of fumarase from Saccharomyces cerevisiae']",4.4.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,1122,1,85-92,"Jan S. Keruchenko, Irina D. Keruchenko, Kirill L. Gladilin, Vyacheslav N. Zaitsev, Nickolai Y. Chirgadze",en
+973,92KIM/KIN,,10.1152/ajpendo.1992.262.3.E344,,-,-,-,-,-,-,-,-,-,-
+974,92KIT/SAS,,10.1271/bbb.56.652,,-,-,-,-,-,-,-,-,-,-
+975,92KRA,,,,-,-,-,-,-,-,-,-,-,-
+976,92LEE/HAN,,,,-,-,-,-,-,-,-,-,-,-
+977,92LOR/TRA,,10.1016/B978-0-444-89046-7.50076-X,,-,-,-,-,-,-,-,-,-,-
+978,92QAM/YOO,1327136.0,10.1021/bi00156a018,,-,-,-,-,-,-,-,-,-,-
+979,92REK/TIS,,,,-,-,-,-,-,-,-,-,-,-
+980,92TEA/DOB,1629208.0,10.1016/S0021-9258(19)49682-8,,['Effect of temperature on the creatine kinase equilibrium.'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,267,20,14084-14093,"W E Teague, G.P. Dobson",en
+981,92WAN/CHE,1633258.0,10.1016/0301-4622(92)80041-3,,['Acetylcholine receptor-enriched membrane vesicles in response to ethanol: Activity and microcalorimetric studies'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,43,1,51-59,"Ying Wang, Chang-Hwei Chen",en
+982,92WED/LEY,8444866.0,10.1016/S0021-9258(18)53478-5,,['Kinetic and regulatory mechanisms for (Escherichia coli) homoserine dehydrogenase-I. Equilibrium isotope exchange kinetics.'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,268,7,4880-4888,"F.C. Wedler, B.W. Ley",en
+983,92WED/LEY1,1547269.0,10.1016/0167-4838(92)90209-V,,['Preferred order random kinetic mechanism for homoserine dehydrogenase of Escherichia coli (Thr-sensitive) aspartokinase/homoserine dehydrogenase-I: equilibrium isotope exchange kinetics'],4.4.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,1119,3,247-249,"Frederick C. Wedler, Brenda W. Ley, Spencer L. Shames, Steven J. Rembish, Daniel L. Kushmaul",en
+984,92XIA/XUE,,,,-,-,-,-,-,-,-,-,-,-
+985,93AND/BUL,8366124.0,10.1016/S0021-9258(19)36592-5,,['UDP-N-acetylglucosamine acyltransferase of Escherichia coli. The first step of endotoxin biosynthesis is thermodynamically unfavorable.'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,268,26,19858-19865,"M.S. Anderson, H.G. Bull, S.M. Galloway, T.M. Kelly, S Mohan, K Radika, C.R. Raetz",en
+986,93BES/REB,8503876.0,10.1042/bj2920425,,-,-,-,-,-,-,-,-,-,-
+987,93BLI/MAR,,10.1016/0141-0229(93)90173-Y,,['Synthesis of β-lactam antibiotics containing α-aminophenylacetyl group in the acyl moiety catalyzed by d-(—)-Phenylglycyl-β-lactamide amidohydrolase'],28.12.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,15,11,965-973,"Alexander M. Blinkovsky, Adam N. Markaryan",en
+988,93BOH/HUT,,10.1016/0040-6031(93)85092-N,,-,-,-,-,-,-,-,-,-,-
+989,93GOL/TEW,,10.1063/1.555939,,-,-,-,-,-,-,-,-,-,-
+990,93HUT/BOH,,10.1016/0040-6031(93)80327-7,,-,-,-,-,-,-,-,-,-,-
+991,93JAN/PAD,18613144.0,10.1002/bit.260420806,,['Solvent effects on lipase‐catalyzed esterification of glycerol and fatty acids'],29.12.2004,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,42,8,953-962,"Anja E. M. Janssen, Albert Van der Padt, Klaas Van't Riet",en
+992,93LAR/TEW,,10.1006/jcht.1993.1009,,"['Thermochemistry of the reactions between adenosine, adenosine 5′-monophosphate, inosine, and inosine 5′-monophosphate; the conversion of d-histidine to (urocanic acid+ammonia)']",18.9.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,25,1,73-90,"J.W. Larson, Y.B. Tewari, R.N. Goldberg",en
+993,93MOC/STR,,10.1016/S0031-9422(00)95139-2,,['Energetics of the uridine 5′-diphosphoglucose: Hydroxycinnamic acid acyl-glucosyltransferase reaction'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,32,3,575-579,"Hans-Peter Mock, Dieter Strack",en
+994,93SHI/CHE,8381432.0,10.1016/S0021-9258(18)53720-0,,['Purification and characterization of novel “2-arylpropionyl-CoA epimerases” from rat liver cytosol and mitochondria.'],5.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,268,5,3487-3493,"W.R. Shieh, C.S. Chen",en
+995,93TEW/KIS,,10.1006/jcht.1993.1028,,['Thermochemistry of the hydrolysis of d-arginine to (d-citrulline+ammonia) and of the hydrolysis of d-arginine to (d-ornithine+urea)'],18.9.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,25,2,293-305,"Y.B. Tewari, N. Kishore, S.A. Margolis, R.N. Goldberg, T. Shibatani",en
+996,93VIN/GRU,7503993.0,10.1016/S0021-9258(19)74485-8,,['A new paradigm for biochemical energy coupling. Salmonella typhimurium nicotinate phosphoribosyltransferase.'],6.1.2021,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,268,34,26004-26010,"A Vinitsky, C Grubmeyer",en
+997,93WER/TWE,16349034.0,10.1128/aem.59.9.2823-2829.1993,,['Purification and Characterization of Maleate Hydratase from\n Pseudomonas pseudoalcaligenes'],1.1.2020,American Society for Microbiology,https://journals.asm.org/non-commercial-tdm-license,journal-article,59,9,2823-2829,"Mari�t J. van der Werf, Will J. J. van den Tweel, Sybe Hartmans",en
+998,93WER/TWE2,8223624.0,10.1111/j.1432-1033.1993.tb18332.x,,['Thermodynamics of the maleate and citraconate hydration reactions catalysed by malease from Pseudomonas pseudoalcaligenes'],4.3.2005,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,217,3,1011-1017,"Mariët J. VAN DER WERF, Will J. J. VAN DEN TWEEL, Sybe HARTMANS",en
+999,93WIL/TOO,,10.1021/jo00065a010,,-,-,-,-,-,-,-,-,-,-
+1000,94CHI/KIR,,10.1016/0167-4838(94)90006-X,,"['α,β-Unsaturated carbonyl compounds: inhibition of rat liver glutathione S-transferase isozymes and chemical reaction with reduced glutathione']",11.2.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,1204,2,175-180,"Cheng-i Chien, Kirollos S. Kirollos, Russell J. Linderman, Walter C. Dauterman",en
+1001,94KIS/TEW,8155816.0,10.1016/0301-4622(93)e0067-f,,['Thermodynamics of the hydrolysis of penicillin G and ampicillin'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,49,2,163-174,"N. Kishore, Y.B. Tewari, W.T. Yap, R.N. Goldberg",en
+1002,94LEU/COO,8117730.0,10.1021/bi00175a040,,-,-,-,-,-,-,-,-,-,-
+1003,94NOE/COL,,10.1016/S0885-5765(05)80059-1,,['Purification and characterization of mannitol dehydrogenase from the fungal tomato pathogen Cladosporium fulvum (syn. Fulvia fulva)'],11.3.2005,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,45,4,281-289,"P.K.M. Noeldner, M.J. Coleman, R. Faulks, R.P. Oliver",en
+1004,94REK/SCH,,10.1021/j100066a032,,-,-,-,-,-,-,-,-,-,-
+1005,94TEW/GOL,,10.1007/BF00973544,,['An equilibrium and calorimetric investigation of the hydrolysis of L-tryptophan to (indole + pyruvate + ammonia)'],13.1.2005,Springer Science and Business Media LLC,http://www.springer.com/tdm,journal-article,23,2,167-184,"Yadu B. Tewari, Robert N. Goldberg",en
+1006,95BIS/KRA,,10.1002/9783527619429.ch4,,-,-,-,-,-,-,-,-,-,-
+1007,95CHE/ARM,,10.1021/tx00046a012,,-,-,-,-,-,-,-,-,-,-
+1008,95GOL/TEW,,10.1063/1.555969,,-,-,-,-,-,-,-,-,-,-
+1009,95HUT/BOH,,10.1016/0040-6031(94)01957-I,,['Calorimetric investigations into enzymatic urea hydrolysis'],1.5.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,250,1,1-12,"Regina Hüttl, Klaus Bohmhammel, Gert Wolf, Ralf Oehmgen",en
+1010,95JUS/KOT,,10.1016/0040-6031(95)90714-9,,-,-,-,-,-,-,-,-,-,-
+1011,95KAM/JUR,,10.1007/BF00301478,,['In vivo nuclear magnetic resonance studies on the lugworm Arenicola marina. I. Free inorganic phosphate and free adenylmonophosphate concentrations in the body wall and their dependence on hypoxia'],9.10.2004,Springer Science and Business Media LLC,http://www.springer.com/tdm,journal-article,165,2,143-152,"G. Kamp, H. -P. Juretschke, U. Thiel, H. Englisch",en
+1012,95KOZ/TOM,,10.1021/ja00113a002,,-,-,-,-,-,-,-,-,-,-
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+1015,95LIA/WAN2,,10.1016/0040-6031(95)02513-8,,-,-,-,-,-,-,-,-,-,-
+1016,95LIU/ZEN,,10.1016/0040-6031(94)02080-8,,-,-,-,-,-,-,-,-,-,-
+1017,95PEL/MAC,7548019.0,10.1021/bi00039a025,,-,-,-,-,-,-,-,-,-,-
+1018,95SCH/TRA,7827041.0,10.1021/bi00003a016,,-,-,-,-,-,-,-,-,-,-
+1019,95TEW/SCH,,10.1021/j100005a034,,-,-,-,-,-,-,-,-,-,-
+1020,95WIS/KUS,7759484.0,10.1074/jbc.270.21.12428,,['Creatine Kinase Equilibration Follows Solution Thermodynamics in Skeletal Muscle.'],26.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,270,21,12428-12438,"Robert W. Wiseman, Martin J. Kushmerick",en
+1021,96ARA/RUZ,8639492.0,10.1021/bi952983w,,-,-,-,-,-,-,-,-,-,-
+1022,96HIR/MAY,,10.5650/jos1996.45.761,,-,-,-,-,-,-,-,-,-,-
+1023,96KIM/DUN,8605214.0,10.1021/bi952944k,,-,-,-,-,-,-,-,-,-,-
+1024,96LI/ZHA,8910414.0,10.1074/jbc.271.45.28038,,['Kinetic and Thermodynamic Characterizations of Yeast Guanylate Kinase'],26.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,271,45,28038-28044,"Yue Li, Yanling Zhang, Honggao Yan",en
+1025,96LIA/WAN,,,,-,-,-,-,-,-,-,-,-,-
+1026,96OES/SCH,,10.1016/S0168-9452(96)04475-5,,['Phosphomannomutase and phosphoglucomutase in the red alga Galdieria sulphuraria'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,121,1,19-27,"Christine Oesterhelt, Claus Schnarrenberger, Wolfgang Gross",en
+1027,96PRO/GRO,,10.1111/j.1399-3054.1996.tb06681.x,,['Purification and characterization of UDP‐D‐galactose 4‐epimerase from the red alga Galdieria sulphuraria'],1.5.2006,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,98,4,753-758,"Pavel V. Prosselkov, Wolfgang Gross, Abir U. Igamberdiev, Claus Schnarrenberger",en
+1028,96TEW/GOL,,10.1006/jcht.1996.0099,,['Thermodynamics of reactions catalyzed byL-iditol 2-dehydrogenase: the xylose assimilation pathway'],6.10.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,28,10,1127-1144,"Yadu B. Tewari, Robert N. Goldberg",en
+1029,96TEW/SCH,,10.1006/jcht.1996.0016,,"['Thermodynamics of the hydrolysis of 3,4,5-trihydroxybenzoic acid propyl ester (n-propylgallate) to 3,4,5-trihydroxybenzoic acid (gallic acid) and propan-1-ol in aqueous media and in toluene']",18.9.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,28,2,171-185,"Yadu B. Tewari, Michele M. Schantz, Mikhail V. Rekharsky, Robert N. Goldberg",en
+1030,97CHA,9326504.0,10.1242/jeb.200.21.2789,,['Mitochondrial arginine kinase in the midgut of the tobacco hornworm (Manduca sexta)'],25.4.2021,The Company of Biologists,http://www.biologists.com/user-licence-1-1/,journal-article,200,21,2789-2796,M. E. Chamberlin,en
+1031,97CON/DEL,,10.1016/S0141-0229(97)00021-5,,['Simultaneous effects of immobilization and substrate protection on the thermodynamics of glucose isomerase activity and inactivation'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,21,7,511-517,"Attilio Converti, Marco Del Borghi",en
+1032,97DEJ/ROC,,10.1007/BF01007697,,"['Purification, characterization and physiological role of sucrose synthase in the pea seed coat (Pisum sativum L.)']",19.1.2005,Springer Science and Business Media LLC,http://www.springer.com/tdm,journal-article,201,2,128-137,"A. D�jardin, C. Rochat, S. Maugenest, J. -P. Boutin",en
+1033,97HAN/KLE,,10.1016/S0167-4838(96)00161-6,,['Purification and characterization of d(+)-carnitine dehydrogenase from Agrobacterium sp. — a new enzyme of carnitine metabolism'],26.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,1337,1,133-142,"Henning Hanschmann, Hans-Peter Kleber",en
+1034,97KAS/TEW,,10.1021/jp972501l,,-,-,-,-,-,-,-,-,-,-
+1035,97LIA/WU,,10.1016/S0040-6031(97)00363-8,,['Thermokinetic models of enzyme-catalyzed reactions in batch and plug-flow reactors'],23.4.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,307,2,149-153,"Yi Liang, Yuanxin Wu, Dinghuo Li, Cunxin Wang, Yi Liu, Songsheng Qu, Guolin Zou",en
+1036,97PES/PRI,,10.1002/(SICI)1097-0290(19971005)56:1<9::AID-BIT2>3.0.CO,,-,-,-,-,-,-,-,-,-,-
+1037,97SAL/GOD,,10.1021/bp9700869,,['Enzymatic Large-Scale Production of 2-Keto-3-deoxy-D-GLYCERO-D-galacto-nonopyranulosonic Acid in Enzyme Membrane Reactors'],26.7.2002,Wiley,http://doi.wiley.com/10.1002/tdm_license_1.1,journal-article,13,6,810-813,"C. Salagnad, A. Godde, B. Ernst, U. Kragl",en
+1038,97STA/SUA,9319107.0,10.1242/jeb.200.8.1247,,['Honeybee Flight Muscle Phosphoglucose Isomerase: Matching Enzyme Capacities to Flux Requirements at a Near-Equilibrium Reaction'],25.4.2021,The Company of Biologists,http://www.biologists.com/user-licence-1-1/,journal-article,200,8,1247-1254,"James F. Staples, Raul K. Suarez",en
+1039,97TEW/GOL,,10.1016/S0008-6215(97)00073-6,,"['Thermodynamics of the hydrolysis and cyclization reactions of α-, β-, and γ-cyclodextrin']",25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,301,1-2,11-22,"Yadu B. Tewari, Robert N. Goldberg, Michikatsu Sato",en
+1040,97XU/EAD,9132023.0,10.1021/bi9616007,,-,-,-,-,-,-,-,-,-,-
+1041,97YOR/ISH,,10.1093/oxfordjournals.jbchem.a021786,,-,-,-,-,-,-,-,-,-,-
+1042,98CON/BOR,,10.1007/s004490050406,,-,-,-,-,-,-,-,-,-,-
+1043,98CON/DEL,,10.1007/s004490050406,,-,-,-,-,-,-,-,-,-,-
+1044,98DIE/STR,,10.1016/S1381-1177(98)00044-7,,['Feasibility of the thermodynamically controlled synthesis of amoxicillin'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,5,1-4,249-253,"M.B. Diender, A.J.J. Straathof, L.A.M. van der Wielen, C. Ras, J.J. Heijnen",en
+1045,98DIE/STR2,,10.3109/10242429809003622,,-,-,-,-,-,-,-,-,-,-
+1046,98KIM/VOE,9506987.0,10.1074/jbc.273.12.6844,,"['Expression, Purification, and Characterization of Choline Kinase, Product of the CKI Gene from Saccharomyces cerevisiae']",26.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,273,12,6844-6852,"Kee-Hong Kim, Dennis R. Voelker, Mark T. Flocco, George M. Carman",en
+1047,98KIS/TEW,9700925.0,10.1016/s0301-4622(98)00151-3,,['A thermodynamic investigation of reactions catalyzed by tryptophan synthase'],26.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,73,3,265-280,"Nand Kishore, Yadu B. Tewari, David L. Akers, Robert N. Goldberg, Edith Wilson Miles",en
+1048,98KIS/TEW2,,10.1006/jcht.1998.0404,,['An investigation of the equilibrium of the reaction {L-aspartate(aq)+2-oxoglutarate(aq)=oxaloacetate(aq)+L-glutamate(aq)}'],6.10.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,30,11,1373-1384,"Nand Kishore, Yadu B. Tewari, Robert N. Goldberg",en
+1049,98LAE/EIS,9738901.0,10.1046/j.1432-1327.1998.2550618.x,,"['Cyclohexa‐1,5‐diene‐1‐carboxyl‐CoA hydratase, an enzyme involved in anaerobic metabolism of benzoyl‐CoA in the denitrifying bacterium Thauera aromatica']",11.3.2003,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,255,3,618-627,"Diana Laempe, Wolfgang Eisenreich, Adelbert Bacher, Georg Fuchs",en
+1050,98LIA/QU,,10.1007/BF02883019,,['Microcalorimetric studies on the dismutation of superoxide anion catalyzed by superoxide dismutase'],7.4.2008,Springer Science and Business Media LLC,http://www.springer.com/tdm,journal-article,41,6,575-586,"Yi Liang, Songsheng Qu, Cunxin Wang, Yuwen Liu, Zhiyong Wang, Zhaohua Song, Guolin Zou",en
+1051,98LIA/WAN,,10.1016/S0040-6031(98)00464-X,,['Thermokinetic method for faster enzyme-catalyzed reactions'],25.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,322,1,1-7,"Yi Liang, Cunxin Wang, Songsheng Qu, Yuanxin Wu, Dinghuo Li, Guolin Zou",en
+1052,98LOV/LAU,9799130.0,10.1046/j.1432-1327.1998.2570286.x,,['Reconsidering the energetics of ribonuclease catalysed RNA hydrolysis'],11.3.2003,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,257,1,286-290,"Stefan Loverix, Georges Laus, José C. Martins, Lode Wyns, Jan Steyaert",en
+1053,98TEW,,10.1021/je980021x,,-,-,-,-,-,-,-,-,-,-
+1054,98TEW/CHE,,10.1021/jp982754u,,-,-,-,-,-,-,-,-,-,-
+1055,98TEW/KIS,,10.1006/jcht.1998.0342,,['An equilibrium and calorimetric study of some transamination reactions'],18.9.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,30,6,777-793,"Yadu B. Tewari, Nand Kishore, Robert N. Goldberg, Tinh N. Luong",en
+1056,98THO/JOR,9466792.0,10.1006/abio.1997.2490,,['Partition Analysis of an Enzyme Acting Concurrently upon Two Substrates in a Continuous Multiwavelength Assay'],19.5.2003,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,256,1,7-13,"James E. Thompson, Douglas B. Jordan",en
+1057,98URB/BRA,9922170.0,10.1021/bi981819g,,-,-,-,-,-,-,-,-,-,-
+1058,99BAS/MAR,10637769.0,10.1080/152165499306630,,-,-,-,-,-,-,-,-,-,-
+1059,99BRA/FIS,10358012.0,10.1074/jbc.274.24.16727,,['Histidine 179 Mutants of GTP Cyclohydrolase I Catalyze the Formation of 2-Amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone Triphosphate'],26.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,274,24,16727-16735,"Andreas Bracher, Markus Fischer, Wolfgang Eisenreich, Harald Ritz, Nicholas Schramek, Peter Boyle, Patrizia Gentili, Robert Huber, Herbert Nar, Günter Auerbach, Adelbert Bacher",en
+1060,99ELS,,,,-,-,-,-,-,-,-,-,-,-
+1061,99GRA/NID,10455186.0,10.1074/jbc.274.35.25069,,"['Characterization of dTDP-4-dehydrorhamnose 3,5-Epimerase and dTDP-4-dehydrorhamnose Reductase, Required for dTDP-l-rhamnose Biosynthesis in Salmonella enterica Serovar Typhimurium LT2']",26.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,274,35,25069-25077,"Michael Graninger, Bernd Nidetzky, David E. Heinrichs, Chris Whitfield, Paul Messner",en
+1062,99HUT/OEH,,10.1016/S0040-6031(98)00547-4,,['Calorimetric investigations of the enzyme catalyzed sucrose hydrolysis'],26.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,325,1,1-4,"Regina Hüttl, Katrin Oehlschläger, Gert Wolf",en
+1063,99KAT/UED,10521704.0,10.1016/S1388-1981(99)00124-9,,['Equilibrium in the hydrolysis and synthesis of cannabimimetic anandamide demonstrated by a purified enzyme'],26.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,1440,2-3,205-214,"Kazuhisa Katayama, Natsuo Ueda, Itsuo Katoh, Shozo Yamamoto",en
+1064,99KIS/HOL,,10.1006/jcht.1998.0444,,['A thermodynamic investigation of some reactions involving prephenic acid'],18.9.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,31,2,211-227,"N Kishore, M.J Holden, Y.B Tewari, R.N Goldberg",en
+1065,99KIS/TEW,,10.1006/jcht.1999.0496,,['A thermodynamic study of the hydrolysis of L-glutamine to (L-glutamate + ammonia) and of L-asparagine to (L -aspartate + ammonia)'],18.9.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,32,9,1077-1090,"Nand Kishore, Yadu B. Tewari, Robert N. Goldberg",en
+1066,99MUN/LOP,10027985.0,10.1046/j.1365-2958.1999.01211.x,,['First molecular characterization of a uridine diphosphate galacturonate 4‐epimerase: an enzyme required for capsular biosynthesis in Streptococcus pneumoniae type 1'],12.3.2003,Wiley,http://onlinelibrary.wiley.com/termsAndConditions#vor,journal-article,31,2,703-713,"Rosario Muñoz, Rubens López, Mercedes De Frutos, Ernesto García",en
+1067,99NIE/SCH,,10.3109/10242429909040115,,-,-,-,-,-,-,-,-,-,-
+1068,99SAK/UTS,10087174.0,10.1006/abbi.1999.1121,,['An AMP-Dependent (ATP-Forming) Kinase in the Hyperthermophilic ArchaeonPyrococcus furiosus:Characterization and Novel Physiological Role'],7.10.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,364,1,125-128,"Haruhiko Sakuraba, Emi Utsumi, Chizu Kujo, Toshihisa Ohshima",en
+1069,99TEA/DOB,10428820.0,10.1074/jbc.274.32.22459,,['Thermodynamics of the Arginine Kinase Reaction'],26.7.2002,Elsevier BV,https://www.elsevier.com/tdm/userlicense/1.0/,journal-article,274,32,22459-22463,"Walter E. Teague, Geoffrey P. Dobson",en
+1070,99TEW/SCH,,10.1021/je980299p,,-,-,-,-,-,-,-,-,-,-
diff --git a/ruslan/DOI2META/openTECRmetadataPubMed.csv b/ruslan/DOI2META/openTECRmetadataPubMed.csv
new file mode 100644
index 0000000..d1e4bf1
--- /dev/null
+++ b/ruslan/DOI2META/openTECRmetadataPubMed.csv
@@ -0,0 +1,1072 @@
+,reference_code,pmid,doi,comment,Language,Volume,Issue,Page,Journal,Abstract,Date,Authors
+0,00BYR/GOL,10723544.0,10.1016/S0301-4622(99)00145-3,,['eng'],84,1,45-64,Biophysical chemistry,"Microcalorimetry and high performance liquid chromatography have been used to conduct a thermodynamic investigation of reactions catalyzed by anthranilate synthase, the enzyme located at the first step in the biosynthetic pathway leading from chorismate to tryptophan. One of the overall biochemical reactions catalyzed by anthranilate synthase is: chorismate(aq) + ammonia(aq) = anthranilate(aq) + pyruvate(aq) + H2O(l). This reaction can be divided into two partial reactions involving the intermediate 2-amino-4-deoxyisochorismate (ADIC): chorismate(aq) + ammonia(aq) = ADIC(aq) + H2O(l) and ADIC(aq) = anthranilate(aq) + pyruvate(aq). The native anthranilate synthase and a mutant form of it that is deficient in ADIC lyase activity but has ADIC synthase activity were used to study the overall ammonia-dependent reaction and the first of the above two partial reactions, respectively. Microcalorimetric measurements were performed on the overall reaction at a temperature of 298.15 K and pH 7.79. Equilibrium measurements were performed on the first partial (ADIC synthase) reaction at temperatures ranging from 288.15 to 302.65 K, and at pH values from 7.76 to 8.08. The results of the equilibrium and calorimetric measurements were analyzed in terms of a chemical equilibrium model that accounts for the multiplicity of ionic states of the reactants and products. These calculations gave thermodynamic quantities at the temperature 298.15 K and an ionic strength of zero for chemical reference reactions involving specific ionic forms. For the reaction: chorismate2-(aq) + NH4+(aq) = anthranilate-(aq) + pyruvate-(aq) + H+(aq) + H2O(l), delta rHmo = -(116.3 +/- 5.4) kJ mol-1. For the reaction: chorismate2-(aq) + NH4+(aq) = ADIC-(aq) + H2O(l), K = (20.3 +/- 4.5) and delta rHmo = (7.5 +/- 0.6) kJ mol-1. Thermodynamic cycle calculations were used to calculate thermodynamic quantities for three additional reactions that are pertinent to this branch point of the chorismate pathway. The quantities obtained in this study permit the calculation of the position of equilibrium of these reactions as a function of temperature, pH, and ionic strength. Values of the apparent equilibrium constants and the standard transformed Gibbs energy changes delta rG'mo under approximately physiological conditions are given.",Feb 2000,"W M Byrnes, R N Goldberg, M J Holden, M P Mayhew, Y B Tewari"
+1,00DIC/BUR,10748184.0,10.1074/jbc.M910044199,"same as 01DIC/BUR, part 7, ref 98",['eng'],275,21,15828-31,The Journal of biological chemistry,"The repair of phosphodiester bonds in nicked DNA is catalyzed by DNA ligases. Ligation is coupled to cleavage of a phosphoanhydride bond in a nucleotide cofactor resulting in a thermodynamically favorable process. A free energy value for phosphodiester bond formation was calculated using the reversibility of the T4 DNA ligase reaction. The relative number of DNA nicks to phosphodiester bonds in a circular plasmid DNA, formed during this reaction at fixed concentrations of ATP to AMP and PP(i), was quantified. At 25 degrees C, pH 7, the equilibrium constant (K(eq)) for the ligation reaction is 3.89 x 10(4) m. This value corresponds to a standard free energy (DeltaG degrees ') of -6.3 kcal mol(-1). By subtracting the known energy contribution due to hydrolysis of ATP to AMP and PP(i), DeltaG degrees ' for the hydrolysis of a DNA phosphodiester bond is -5.3 kcal mol(-1).",May 2000,"K S Dickson, C M Burns, J P Richardson"
+2,00DIE,,,"part 7, ref 150",-,-,-,-,-,-,-,-
+3,00FLO/SEW,10620267.0,10.1002/(SICI)1097-0290(20000205)67:3<364::AID-BIT13>3.0.CO,,['eng'],67,3,364-71,Biotechnology and bioengineering,"The equilibrium position in lipase mediated esterification of various fatty acids and butanol was studied. The influence of the chain length and the presence of unsaturations in the fatty acids on the equilibrium position was measured and predicted. To predict equilibrium position the program TREP extended (TREPEX) based on the UNIFAC group contribution method was used. Using an equilibrium constant of 35, calculated on the basis of thermodynamic activities, the equilibrium position between butanol and saturated and/or unsaturated fatty acids with different chain lengths can be predicted. The ester mole fraction at equilibrium increases with the fatty acid chain length, and for fatty acids with the same carbon number, the highest values are found for unsaturated fatty acids. For reaction systems containing two saturated fatty acids, a slightly higher mole fraction is obtained for the fatty acid with the higher chain length, while for mixtures consisting of saturated and unsaturated fatty acids, the mole fractions of the unsaturated esters are lower than those of the saturated ones, regardless the chain length of the fatty acid. These experimental results are in good agreement with the calculations with TREPEX.",Feb 2000,"M V Flores, J J Sewalt, A E Janssen, A van der Padt"
+4,00FRA/KOS,,10.1039/b000018n,,-,-,-,-,-,-,-,-
+5,00KIS/TEW,,10.1006/jcht.1999.0496,,-,-,-,-,-,-,-,-
+6,00LIA/HUA,,10.1016/S0040-6031(00)00355-5,,-,-,-,-,-,-,-,-
+7,00LIA/QU,,10.1016/S0009-2509(00)00417-6,,-,-,-,-,-,-,-,-
+8,00ROD/BAR,10890880.0,10.1073/pnas.120168097,,['eng'],97,15,8705-10,Proceedings of the National Academy of Sciences of the United States of America,"A distinct phosphodiesterasic activity (EC 3.1.4) was found in both mono- and dicotyledonous plants that catalyzes the hydrolytic breakdown of ADPglucose (ADPG) to produce equimolar amounts of glucose-1-phosphate and AMP. The enzyme responsible for this activity, referred to as ADPG pyrophosphatase (AGPPase), was purified over 1,100-fold from barley leaves and subjected to biochemical characterization. The calculated K(eq)' (modified equilibrium constant) value for the ADPG hydrolytic reaction at pH 7.0 and 25 degrees C is 110, and its standard-state free-energy change value (DeltaG') is -2.9 kcal/mol (1 kcal = 4.18 kJ). Kinetic analyses showed that, although AGPPase can hydrolyze several low-molecular weight phosphodiester bond-containing compounds, ADPG proved to be the best substrate (K(m) = 0.5 mM). P(i) and phosphorylated compounds such as 3-phosphoglycerate, PP(i), ATP, ADP, NADP(+), and AMP are inhibitors of AGPPase. Subcellular localization studies revealed that AGPPase is localized exclusively in the plastidial compartment of cultured cells of sycamore (Acer pseudoplatanus L.), whereas it occurs both inside and outside the plastid in barley endosperm. In this paper, evidence is presented that shows that AGPPase, whose activity declines concomitantly with the accumulation of starch during development of sink organs, competes with starch synthase (ADPG:1,4-alpha-d-glucan 4-alpha-d-glucosyltransferase; EC) for ADPG, thus markedly blocking the starch biosynthesis.",Jul 2000,"M Rodriguez-López, E Baroja-Fernández, A Zandueta-Criado, J Pozueta-Romero"
+9,00TEW,,10.1016/S1381-1177(99)00087-9,,-,-,-,-,-,-,-,-
+10,00TEW/DAV,,10.1006/jcht.2000.0677,,-,-,-,-,-,-,-,-
+11,00TEW/GOL,,10.1006/jcht.2000.0686,,-,-,-,-,-,-,-,-
+12,00WU/FEN,,10.1021/ja992286h,,-,-,-,-,-,-,-,-
+13,00ZHE/BLA,10736170.0,10.1021/bi992676g,,['eng'],39,13,3708-17,Biochemistry,"Ketopantoate reductase (EC 1.1.1.169) catalyzes the NADPH-dependent reduction of alpha-ketopantoate to form D-(-)-pantoate in the pantothenate/coenzyme A biosynthetic pathway. The enzyme encoded by the panE gene from E. coli K12 was overexpressed and purified to homogeneity. The native enzyme exists in solution as a monomer with a molecular mass of 34 000 Da. The steady-state initial velocity and product inhibition patterns are consistent with an ordered sequential kinetic mechanism in which NADPH binding is followed by ketopantoate binding, and pantoate release precedes NADP(+) release. The pH dependence of the kinetic parameters V and V/K for substrates in both the forward and reverse reactions suggests the involvement of a single general acid/base in the catalytic mechanism. An enzyme group exhibiting a pK value of 8.4 +/- 0.2 functions as a general acid in the direction of the ketopantoate reduction, while an enzyme group exhibiting a pK value of 7.8 +/- 0.2 serves as a general base in the direction of pantoate oxidation. The stereospecific transfer of the pro-S hydrogen atom of NADPH to the C-2 position of ketopantoate was demonstrated by (1)H NMR spectroscopy. Primary deuterium kinetic isotope effects of 1.3 and 1.5 on V(for) and V/K(NADPH), respectively, and 2.1 and 1.3 on V(rev) and V/K(HP), respectively, suggest that hydride transfer is not rate-limiting in catalysis. Solvent kinetic isotope effects of 1.3 on both V(for) and V/K(KP), and 1.4 and 1.5 on V(rev) and V/K(HP), respectively, support this conclusion. The apparent equilibrium constant, K(eq)', of 676 at pH 7.5 and the standard free energy change, DeltaG, of -14 kcal/mol suggest that ketopantoate reductase reaction is very favorable in the physiologically important direction of pantoate formation.",Apr 2000,"R Zheng, J S Blanchard"
+14,01TEW/BUN,,10.1016/S1381-1177(01)00016-9,,-,-,-,-,-,-,-,-
+15,01TEW/KIS,,10.1006/jcht.2001.0862,,-,-,-,-,-,-,-,-
+16,01TIS/IHL,,,,-,-,-,-,-,-,-,-
+17,02DOB/HIT,11986306.0,10.1074/jbc.M111422200,,['eng'],277,30,27176-82,The Journal of biological chemistry,"The effect of temperature, pH, and free [Mg(2+)] on the apparent equilibrium constant of pyruvate kinase (phosphoenol transphosphorylase) (EC ) was investigated. The apparent equilibrium constant, K', for the biochemical reaction P-enolpyruvate + ADP = ATP + Pyr was defined as K' = [ATP][Pyr]/[ADP][P-enolpyruvate], where each reactant represents the sum of all the ionic and metal complexed species in M. The K' at pH 7.0, 1.0 mm free Mg(2+) and I of 0.25 m was 3.89 x 10(4) (n = 8) at 25 degrees C. The standard apparent enthalpy (DeltaH' degrees ) for the biochemical reaction was -4.31 kJmol(-1) in the direction of ATP formation. The corresponding standard apparent entropy (DeltaS' degrees ) was +73.4 J K(-1) mol(-1). The DeltaH degrees and DeltaS degrees values for the reference reaction, P-enolpyruvate(3-) + ADP(3-) + H(+) = ATP(4-) + Pyr(1-), were -6.43 kJmol(-1) and +180 J K(-1) mol(-1), respectively (5 to 38 degrees C). We examined further the mass action ratio in rat heart and skeletal muscle at rest and found that the pyruvate kinase reaction in vivo was close to equilibrium i.e. within a factor of about 3 to 6 of K' in the direction of ATP at the same pH, free [Mg(2+)], and T. We conclude that the pyruvate kinase reaction may be reversed under some conditions in vivo, a finding that challenges the long held dogma that the reaction is displaced far from equilibrium.",Jul 2002,"Geoffrey P Dobson, Sam Hitchins, Walter E Teague"
+18,02FLO/HAL,12001171.0,10.1002/bit.10260,,['eng'],78,7,795-801,Biotechnology and bioengineering,"A kinetic model derived from the ping-pong bi-bi reversible mechanism is proposed to described the acylation of glucose by lauric acid in 2-methyl 2-butanol mediated by Candida antarctica lipase at 60 degrees C. The model accounts for the effect of all four compounds in the reaction mixture, namely lauric acid, glucose, water, and lauroyl glucose ester. A supersaturated glucose solution was used to avoid limitations by glucose dissolution rate. Experiments with varied initial water content were performed to determine the effect of water on the initial reaction rate. The full time course of ester formation is described by five parameters: (a) three parameters evaluated from initial rate measurements; (b) the equilibrium constant, independently evaluated; and (c) one extra parameter fitted to the progress curve of ester formation. This reduced form of a full reversible kinetic model based on the ping-pong bi-bi mechanism is able to describe the complete course of lauroyl glucose ester synthesis. The proposed model provides a good fit for the experimental results.",Jun 2002,"Maria Victoria Flores, Peter J Halling"
+19,02ISO/KOI,,10.1016/S1389-1723(02)80173-6,,-,-,-,-,-,-,-,-
+20,02KIM/BAK,12107130.0,10.1128/JB.184.15.4134-4140.2002,,['eng'],184,15,4134-40,Journal of bacteriology,"The 2-aminoethylphosphonate transaminase (AEPT; the phnW gene product) of the Salmonella enterica serovar Typhimurium 2-aminoethylphosphonate (AEP) degradation pathway catalyzes the reversible reaction of AEP and pyruvate to form phosphonoacetaldehyde (P-Ald) and L-alanine (L-Ala). Here, we describe the purification and characterization of recombinant AEPT. pH rate profiles (log V(m) and log V(m)/K(m) versus pH) revealed a pH optimum of 8.5. At pH 8.5, K(eq) is equal to 0.5 and the k(cat) values of the forward and reverse reactions are 7 and 9 s(-1), respectively. The K(m) for AEP is 1.11 +/- 0.03 mM; for pyruvate it is 0.15 +/- 0.02 mM, for P-Ald it is 0.09 +/- 0.01 mM, and for L-Ala it is 1.4 +/- 0.03 mM. Substrate specificity tests revealed a high degree of discrimination, indicating a singular physiological role for the transaminase in AEP degradation. The 40-kDa subunit of the homodimeric enzyme is homologous to other members of the pyridoxalphosphate-dependent amino acid transaminase superfamily. Catalytic residues conserved within well-characterized members are also conserved within the seven known AEPT sequences. Site-directed mutagenesis demonstrated the importance of three selected residues (Asp168, Lys194, and Arg340) in AEPT catalysis.",Aug 2002,"Alexander D Kim, Angela S Baker, Debra Dunaway-Mariano, W W Metcalf, B L Wanner, Brian M Martin"
+21,02NES/ZHO,12133002.0,10.1042/bj20020551,,['eng'],367,Pt 3,587-99,The Biochemical journal,"CHO 2, encoding human sterol 8-isomerase (hSI), was introduced into plasmids pYX213 or pET23a. The resulting native protein was overexpressed in erg 2 yeast cells and purified to apparent homogeneity. The enzyme exhibited a K (m) of 50 microM and a turnover number of 0.423 s(-1) for zymosterol, an isoelectric point of 7.70, a native molecular mass of 107000 Da and was tetrameric. The structural features of zymosterol provided optimal substrate acceptability. Biomimetic studies of acid-catalysed isomerization of zymosterol resulted in formation of cholest-8(14)-enol, whereas the enzyme-generated product was a Delta(7)-sterol, suggesting absolute stereochemical control of the reaction by hSI. Using (2)H(2)O and either zymosterol or cholesta-7,24-dienol as substrates, the reversibility of the reaction was confirmed by GC-MS of the deuterated products. The positional specific incorporation of deuterium at C-9alpha was established by a combination of (1)H- and (13)C-NMR analyses of the enzyme-generated cholesta-7,24-dienol. Kinetic analyses indicated the reaction equilibrium ( K (eq)=14; DeltaG(o')=-6.5 kJ/mol) for double-bond isomerization favoured the forward direction, Delta(8) to Delta(7). Treatment of hSI with different high-energy intermediate analogues produced the following dissociation constants ( K (i)): emopamil (2 microM)=tamoxifen (1 microM)=tridemorph (1 microM)<25-azacholesterol (21 microM) G6P) by baker's yeast phosphoglucose isomerase (PGI) with regard to k(cat) and K(m) were determined from analysis of differential stopped flow microcalorimeter measurements using the integrated form of the Michaelis-Menten rate equation. Values for K(m) (F6P --> G6P) that were determined at pH 8.0 and ionic strength 0.1M at 293.4, 298.4, 303.4, and 311.5K exhibited a linear dependence on the substrate concentration at each temperature because of the substrate-product equilibrium. The minimum values for K(m) ranged from 2.62+/-0.55 mM at 293.4K to 7.8+/-4.8mM at 311.5K and were the same as the minimum values for the reverse reaction (G6P --> F6P) at 293.4 K and 298.4 K. Minimum values for k(cat) increased with temperature, from 2.78+/-0.34s(-1) at 293.4K to 11.4+/-1.0s(-1) at 311.5K, and for the reverse reaction, G6P --> F6P, from 0.852+/-0.086 s(-1) at 293.4K to 1.46+/-0.06s(-1) at 298.4K. The enzyme efficiency at 311.5K is close to the collision rate for a diffusion-controlled process in solution. The [F6P]/[G6P] equilibrium constants were determined from comparison of the values of k(cat) in both directions and were 0.307+/-0.053 at 293.4K and 0.395+/-0.033 at 298.4K. The heats of reaction in the F6P --> G6P direction increased from -8.96+/-0.26 kJmol(-1) at 311.5K to -8.27+/-0.40 kJmol(-1) at 293.4K, a value in fair agreement with 7.01+/-0.32 kJmol(-1) in the opposite G6P --> F6P direction.",Jun 2004,"Magnus Stödeman, Frederick P Schwarz"
+36,04TEW/IHA,,10.1016/j.molcatb.2004.04.005,,-,-,-,-,-,-,-,-
+37,05SIR/HUE,,10.1016/j.tca.2004.06.011,,-,-,-,-,-,-,-,-
+38,05TEW/GOL,,10.1016/j.jct.2004.11.011,,-,-,-,-,-,-,-,-
+39,05TEW/SCH,,10.1016/j.jct.2004.08.002,,-,-,-,-,-,-,-,-
+40,06AIR,16427818.0,10.1016/j.bbapap.2005.11.020,,['eng'],1764,2,307-19,Biochimica et biophysica acta,"A kinetic analysis of the arginyl-tRNA synthetase (ArgRS) from Escherichia coli was accomplished with the goal of improving the rate equations so that they correspond more closely to the experimental results. 22 different steady-state kinetic two-ligand experiments were statistically analysed simultaneously. A mechanism and values for the ArgRS constants were found where the average error was only 6.2% and ranged from 2.5 to 11.2% in the different experiments. The mechanism included not only the normal activation and transfer reactions but also an additional step which may be a conformational change after the transfer reaction but before the dissociation of the product Arg-tRNA from the enzyme. The forward rate constants in these four steps were low, 8.3-27 s(-1), but the reverse rate constants of the activation and transfer reactions were considerably higher (230 and 161 s(-1)). Therefore, in the presence of even low concentrations of PP(i) and AMP, the rate limitation occurs at the late steps of the total reaction. AMP increases the rate of the ATP-PP(i) exchange reaction due to the high reverse rate in the transfer reaction. The rate equation obtained was used to calculate the steady-state enzyme intermediate concentrations and rates between the intermediates. Three different Mg2+ binding sites were required to describe the Mg2+ dependence. One of them was the normal binding to ATP and the others to tRNA or enzyme. The measured Mg2+ dependence of the apparent equilibrium constant of the ArgRS reaction was consistent with the Mg2+ dependences of the reaction rates on the rate equation. Chloride inhibits the ArgRS reaction, 160 mM KCl caused a 50% inhibition if the ionic strength was kept constant with K-acetate. KCl strongly affected the K(m)(app) (tRNA) value. A difference was detected in the progress curves between the aminoacylation and ATP-PP(i) exchange rates. When all free tRNA(Arg) had been used from the reaction mixture, the aminoacylation reaction stopped, but the ATP-PP(i) exchange continued at a lowered rate.",Feb 2006,R Kalervo Airas
+41,06MCC/ARA,16519510.0,10.1021/bi052232m,,['eng'],45,10,3154-62,Biochemistry,"The X-ray crystal structure of the At5g18200.1 protein has been determined to a nominal resolution of 2.30 A. The structure has a histidine triad (HIT)-like fold containing two distinct HIT-like motifs. The sequence of At5g18200.1 indicates a distant family relationship to the Escherichia coli galactose-1-P uridylyltransferase (GalT): the determined structure of the At5g18200.1 protein confirms this relationship. The At5g18200.1 protein does not demonstrate GalT activity but instead catalyzes adenylyl transfer in the reaction of ADP-glucose with various phosphates. The best acceptor among those evaluated is phosphate itself; thus, the At5g18200.1 enzyme appears to be an ADP-glucose phosphorylase. The enzyme catalyzes the exchange of (14)C between ADP-[(14)C]glucose and glucose-1-P in the absence of phosphate. The steady state kinetics of exchange follows the ping-pong bi-bi kinetic mechanism, with a k(cat) of 4.1 s(-)(1) and K(m) values of 1.4 and 83 microM for ADP-[(14)C]glucose and glucose-1-P, respectively, at pH 8.5 and 25 degrees C. The overall reaction of ADP-glucose with phosphate to produce ADP and glucose-1-P follows ping-pong bi-bi steady state kinetics, with a k(cat) of 2.7 s(-)(1) and K(m) values of 6.9 and 90 microM for ADP-glucose and phosphate, respectively, at pH 8.5 and 25 degrees C. The kinetics are consistent with a double-displacement mechanism that involves a covalent adenylyl-enzyme intermediate. The X-ray crystal structure of this intermediate was determined to 1.83 A resolution and shows the AMP group bonded to His(186). The value of K(eq) in the direction of ADP and glucose-1-P formation is 5.0 at pH 7.0 and 25 degrees C in the absence of a divalent metal ion, and it is 40 in the presence of 1 mM MgCl(2).",Mar 2006,"Jason G McCoy, Abolfazl Arabshahi, Eduard Bitto, Craig A Bingman, Frank J Ruzicka, Perry A Frey, George N Phillips"
+42,06ONO/YAN,16616264.0,10.1016/j.phytochem.2006.02.017,,['eng'],67,9,856-60,Phytochemistry,"We demonstrated several kinds of D-amino acids in plant seedlings, and moreover alanine racemase (E.C.5.1.1.1) in alfalfa (Medicago sativa L.) seedlings. This is the first evidence for the presence of amino acid racemase in plant. The enzyme was effectively induced by the addition of L- or D-alanine, and we highly purified the enzyme to show enzymological properties. The enzyme exclusively catalyzed racemization of L- and D-alanine. The K(m) and V(max) values of enzyme for L-alanine were 29.6 x 10(-3) M and 1.02 mol/s/kg, and those for D-alanine are 12.0 x 10(-3) M and 0.44 mol/s/kg, respectively. The K(eq) value was estimated to be about 1 and indicated that the enzyme catalyzes a typical racemization of both enantiomers of alanine. The enzyme was inactivated by hydroxylamine, phenylhydrazine and some other pyridoxal 5'-phosphate enzyme inhibitors. Accordingly, the enzyme required pyridoxal 5'-phosphate as a coenzyme, and enzymologically resembled bacterial alanine racemases studied so far.",May 2006,"Kazutoshi Ono, Kazuki Yanagida, Tadao Oikawa, Tadashi Ogawa, Kenji Soda"
+43,06POD/BEL,16884305.0,10.1021/jm060202r,,['eng'],49,16,4937-45,Journal of medicinal chemistry,"Inhibitors of orotidine monophosphate decarboxylase (ODCase) have applications in RNA viral, parasitic, and other infectious diseases. ODCase catalyzes the decarboxylation of orotidine monophosphate (OMP), producing uridine monophosphate (UMP). Novel inhibitors 6-amino-UMP and 6-cyano-UMP were designed on the basis of the substructure volumes in the substrate OMP and in an inhibitor of ODCase, barbituric acid monophosphate, BMP. A new enzyme assay method using isothermal titration calorimetry (ITC) was developed to investigate the inhibition kinetics of ODCase. The reaction rates were measured by monitoring the heat generated during the decarboxylation reaction of orotidine monophosphate. Kinetic parameters (k(cat) = 21 s(-1) and KM = 5 microM) and the molar enthalpy (DeltaH(app) = 5 kcal/mol) were determined for the decarboxylation of the substrate by ODCase. Competitive inhibition of the enzyme was observed and the inhibition constants (Ki) were determined to be 12.4 microM and 29 microM for 6-aza-UMP and 6-cyano-UMP, respectively. 6-Amino-UMP was found to be among the potent inhibitors of ODCase, having an inhibition constant of 840 nM. We reveal here the first inhibitors of ODCase designed by the principles of bioisosterism and a novel method of using isothermal calorimetry for enzyme inhibition studies.",Aug 2006,"Ewa Poduch, Angelica M Bello, Sishi Tang, Masahiro Fujihashi, Emil F Pai, Lakshmi P Kotra"
+44,06TAN/SUR,16967985.0,10.1021/ja0627702,,['eng'],128,37,12331-8,Journal of the American Chemical Society,"Acetyl-CoA synthase/carbon monoxide dehydrogenase is a Ni-Fe-S-containing enzyme that catalyzes the synthesis of acetyl-CoA from CO, CoA, and a methyl group. The methyl group is transferred onto the enzyme from a corrinoid-iron-sulfur protein (CoFeSP). The kinetics of two steps within the catalytic mechanism were studied using the stopped-flow method, including the insertion of CO into a putative Ni(2+)-CH(3) bond and the transfer of the resulting acetyl group to CoA. Neither step had been studied previously. Reactions were monitored indirectly, starting with the methylated intermediate form of the enzyme. Resulting traces were analyzed by constructing a simple kinetic model describing the catalytic mechanism under reducing conditions. Besides methyl group transfer, CO insertion, and acetyl group transfer, fitting to experimental traces required the inclusion of an inhibitory step in which CO reversibly bound to the form of the enzyme obtained immediately after product release. Global simulation of the reported datasets afforded a consistent set of kinetic parameters. The equilibrium constant for the overall synthesis of acetyl-CoA was estimated and compared to the product of the individual equilibrium constants. Simulations obtained with the model duplicated the essential behavior of the enzyme, in terms of the variation of activity with [CO], and the time-dependent decay of the NiFeC EPR signal upon reaction with CoFeSP. Under standard assay conditions, the model suggests that the vast majority of active enzyme molecules in a population should be in the methylated form, suggesting that the subsequent catalytic step, namely CO insertion, is rate limiting. This conclusion is further supported by a sensitivity analysis showing that the rate is most sensitively affected by a change in the rate coefficient associated with the CO insertion step.",Sep 2006,"Xiangshi Tan, Ivan V Surovtsev, Paul A Lindahl"
+45,06TEW/KIS,,10.1016/j.jct.2005.12.014,,-,-,-,-,-,-,-,-
+46,06TEW/PHI,,10.1016/j.jct.2005.06.005,,-,-,-,-,-,-,-,-
+47,06XU/WES,17002315.0,10.1021/bi0610808,,['eng'],45,39,12156-66,Biochemistry,"Kinetic data have been measured for the histidine-tagged saccharopine dehydrogenase from Saccharomyces cerevisiae, suggesting the ordered addition of nicotinamide adenine dinucleotide (NAD) followed by saccharopine in the physiologic reaction direction. In the opposite direction, the reduced nicotinamide adenine dinucleotide (NADH) adds to the enzyme first, while there is no preference for the order of binding of alpha-ketoglutarate (alpha-Kg) and lysine. In the direction of saccharopine formation, data also suggest that, at high concentrations, lysine inhibits the reaction by binding to free enzyme. In addition, uncompetitive substrate inhibition by alpha-Kg and double inhibition by NAD and alpha-Kg suggest the existence of an abortive E:NAD:alpha-Kg complex. Product inhibition by saccharopine is uncompetitive versus NADH, suggesting a practical irreversibility of the reaction at pH 7.0 in agreement with the overall K(eq). Saccharopine is noncompetitive versus lysine or alpha-Kg, suggesting the existence of both E:NADH:saccharopine and E:NAD:saccharopine complexes. NAD is competitive versus NADH, and noncompetitive versus lysine and alpha-Kg, indicating the combination of the dinucleotides with free enzyme. Dead-end inhibition studies are also consistent with the random addition of alpha-Kg and lysine. Leucine and oxalylglycine serve as lysine and alpha-Kg dead-end analogues, respectively, and are uncompetitive against NADH and noncompetitive against alpha-Kg and lysine, respectively. Oxaloacetate (OAA), pyruvate, and glutarate behave as dead-end analogues of lysine, which suggests that the lysine-binding site has a higher affinity for keto acid analogues than does the alpha-Kg site or that dicarboxylic acids have more than one binding mode on the enzyme. In addition, OAA and glutarate also bind to free enzyme as does lysine at high concentrations. Glutarate gives S-parabolic noncompetitive inhibition versus NADH, indicating the formation of a E:(glutarate)2 complex as a result of occupying both the lysine- and alpha-Kg-binding sites. Pyruvate, a slow alternative keto acid substrate, exhibits competitive inhibition versus both lysine and alpha-Kg, suggesting the combination to the E:NADH:alpha-Kg and E:NADH:lysine enzyme forms. The equilibrium constant for the reaction has been measured at pH 7.0 as 3.9 x 10(-7) M by monitoring the change in NADH upon the addition of the enzyme. The Haldane relationship is in very good agreement with the directly measured value.",Oct 2006,"Hengyu Xu, Ann H West, Paul F Cook"
+48,07LIN/ALG,17223711.0,10.1021/bi062067q,,['eng'],46,3,890-8,Biochemistry,"The kinetic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae was determined using initial velocity studies in the absence and presence of product and dead end inhibitors in both reaction directions. Data suggest a steady state random kinetic mechanism. The dissociation constant of the Mg-homoisocitrate complex (MgHIc) was estimated to be 11 +/- 2 mM as measured using Mg2+ as a shift reagent. Initial velocity data indicate the MgHIc complex is the reactant in the direction of oxidative decarboxylation, while in the reverse reaction direction, the enzyme likely binds uncomplexed Mg2+ and alpha-ketoadipate. Curvature is observed in the double-reciprocal plots for product inhibition by NADH and the dead-end inhibition by 3-acetylpyridine adenine dinucleotide phosphate when MgHIc is the varied substrate. At low concentrations of MgHIc, the inhibition by both nucleotides is competitive, but as the MgHIc concentration increases, the inhibition changes to uncompetitive, consistent with a steady state random mechanism with preferred binding of MgHIc before NAD. Release of product is preferred and ordered with respect to CO2, alpha-ketoadipate, and NADH. Isocitrate is a slow substrate with a rate (V/E(t)) 216-fold slower than that measured with HIc. In contrast to HIc, the uncomplexed form of isocitrate and Mg2+ bind to the enzyme. The kinetic mechanism in the direction of oxidative decarboxylation of isocitrate, on the basis of initial velocity studies in the absence and presence of dead-end inhibitors, suggests random addition of NAD and isocitrate with Mg2+ binding before isocitrate in rapid equilibrium, and the mechanism approximates rapid equilibrium random. The Keq for the overall reaction measured directly using the change in NADH as a probe is 0.45 M.",Jan 2007,"Ying Lin, Susan S Alguindigue, Jerome Volkman, Kenneth M Nicholas, Ann H West, Paul F Cook"
+49,07TEW/KIS,,10.1016/j.jct.2006.10.010,,-,-,-,-,-,-,-,-
+50,07TEW/LIE,,10.1016/j.jct.2006.12.007,,-,-,-,-,-,-,-,-
+51,26QUA/WOO,16743691.0,10.1042/bj0200545,,['eng'],20,3,545-55,The Biochemical journal,-, 1926,"J H Quastel, B Woolf"
+52,29WOO,16744231.0,10.1042/bj0230472,,['eng'],23,3,472-82,The Biochemical journal,-, 1929,B Woolf
+53,31BOR/SCH,,10.1016/S0021-9258(17)32602-9,,-,-,-,-,-,-,-,-
+54,34JAC,,,,-,-,-,-,-,-,-,-
+55,34LOH/MEY,,,,-,-,-,-,-,-,-,-
+56,34MEY/LOH,,,,-,-,-,-,-,-,-,-
+57,35AKA,,,,-,-,-,-,-,-,-,-
+58,35JAC/TAP,,,,-,-,-,-,-,-,-,-
+59,35MEY,,,,-,-,-,-,-,-,-,-
+60,35MEY/KIE,,,,-,-,-,-,-,-,-,-
+61,35MEY/KIE2,,,,-,-,-,-,-,-,-,-
+62,35MEY/LOH,,,,-,-,-,-,-,-,-,-
+63,35MEY/SCH,,,,-,-,-,-,-,-,-,-
+64,36EUL/ADL,,10.1515/bchm2.1936.241.6.239,,-,-,-,-,-,-,-,-
+65,36LEH,,,,-,-,-,-,-,-,-,-
+66,36MEY/LOH,,,,-,-,-,-,-,-,-,-
+67,36MEY/SCH,,,,-,-,-,-,-,-,-,-
+68,36VEI,,,,-,-,-,-,-,-,-,-
+69,37ADL/SRE,,10.1515/bchm2.1937.249.1.24,,-,-,-,-,-,-,-,-
+70,37EUL/ADL,,10.1515/bchm2.1937.247.1-2.65,,-,-,-,-,-,-,-,-
+71,37EUL/ADL2,,10.1515/bchm2.1937.249.1.1,,-,-,-,-,-,-,-,-
+72,37EUL/ADL3,,10.1515/bchm2.1937.245.5-6.217,,-,-,-,-,-,-,-,-
+73,37NEG/WUL,,,,-,-,-,-,-,-,-,-
+74,37STU,,10.1021/ja01287a037,,-,-,-,-,-,-,-,-
+75,38EUL/ADL,,10.1515/bchm2.1938.254.2.61,,-,-,-,-,-,-,-,-
+76,38MEY/SCH,,,,-,-,-,-,-,-,-,-
+77,38SCH/HEL,,10.1002/cber.19380710717,,-,-,-,-,-,-,-,-
+78,39COH,16747057.0,10.1042/bj0331478,,['eng'],33,9,1478-87,The Biochemical journal,-,Sep 1939,P P Cohen
+79,40COH,,10.1016/S0021-9258(18)73021-4,,-,-,-,-,-,-,-,-
+80,40HER/GOR,16747255.0,10.1042/bj0341108,,['eng'],34,7,1108-23,The Biochemical journal,-,Jul 1940,"D Herbert, H Gordon, V Subrahmanyan, D E Green"
+81,40KRE/SMY,16747248.0,10.1042/bj0341041,,['eng'],34,7,1041-5,The Biochemical journal,-,Jul 1940,"H A Krebs, D H Smyth, E A Evans"
+82,41UTT/WER,16560478.0,10.1128/jb.42.5.665-676.1941,,['eng'],42,5,665-76,Journal of bacteriology,-,Nov 1941,"M F Utter, C H Werkman"
+83,41WAR/CHR,,,,-,-,-,-,-,-,-,-
+84,42COL/SUT,,10.1016/S0021-9258(18)72525-8,,-,-,-,-,-,-,-,-
+85,42LEN/STR,,,,-,-,-,-,-,-,-,-
+86,43BAN,,,,-,-,-,-,-,-,-,-
+87,43DOU,,10.1016/S0021-9258(18)44907-1,,-,-,-,-,-,-,-,-
+88,43KAL,,10.1016/S0021-9258(18)72325-9,,-,-,-,-,-,-,-,-
+89,43KRE/EGG,16747647.0,10.1042/bj0370334,,['eng'],37,3,334-8,The Biochemical journal,-,Sep 1943,"H A Krebs, L V Eggleston"
+90,43KUB/OTT,,,,-,-,-,-,-,-,-,-
+91,43MEY/JUN,,10.1016/S0021-9258(18)72218-7,,-,-,-,-,-,-,-,-
+92,44LIP,,10.1016/S0021-9258(18)43172-9,,-,-,-,-,-,-,-,-
+93,45DAR,,10.1111/j.1748-1716.1945.tb00300.x,,-,-,-,-,-,-,-,-
+94,45DRA/MEY,,10.1016/S0021-9258(18)51091-7,,-,-,-,-,-,-,-,-
+95,45GRE/LEL,21006939.0,10.1016/S0021-9258(17)41491-8,,['eng'],161,-,559-82,The Journal of biological chemistry,-,Dec 1945,"D E GREEN, L F LELOIR, V NOCITO"
+96,45OHL,,10.1515/bchm2.1947.282.1-2.37,,-,-,-,-,-,-,-,-
+97,46OHL,,10.1515/zna-1946-0108,appears in part 3 and in part 4,-,-,-,-,-,-,-,-
+98,46OHL2,,10.1515/zna-1946-0107,appears in part 3,-,-,-,-,-,-,-,-
+99,47BUC,,10.1016/0006-3002(47)90143-1,,-,-,-,-,-,-,-,-
+100,47KAL,20285041.0,10.1016/S0021-9258(17)30999-7,,['eng'],167,2,461-75,The Journal of biological chemistry,-,Feb 1947,H M KALCKAR
+101,47MEY/OES,,10.1016/S0021-9258(17)34929-3,,-,-,-,-,-,-,-,-
+102,48KOR,18098602.0,10.1016/S0021-9258(18)57167-2,,['eng'],176,3,1475,The Journal of biological chemistry,-,Dec 1948,A KORNBERG
+103,48OCH,18914071.0,10.1016/S0021-9258(18)57383-X,,['eng'],174,1,133-57,The Journal of biological chemistry,-,May 1948,S OCHOA
+104,48SCO/POW,18909182.0,10.1021/ja01183a070,,['eng'],70,3,1104-7,Journal of the American Chemical Society,-,Mar 1948,"E M SCOTT, R POWELL"
+105,48SOR/DEG,,,,-,-,-,-,-,-,-,-
+106,49BAR,18135786.0,10.1016/S0021-9258(18)56670-9,,['eng'],180,2,535-41,The Journal of biological chemistry,-,Sep 1949,T BARANOWSKI
+107,49HES,18135821.0,10.1016/S0021-9258(18)56708-9,,['eng'],180,2,879-81,The Journal of biological chemistry,-,Sep 1949,S HESTRIN
+108,49MEY/GRE,18116987.0,10.1016/S0021-9258(18)56882-4,,['eng'],178,2,655-67,The Journal of biological chemistry,-,Apr 1949,"O MEYERHOF, H GREEN"
+109,49MEY/OES,18134595.0,10.1016/S0021-9258(18)56800-9,,['eng'],179,3,1371-85,The Journal of biological chemistry,-,Jul 1949,"O MEYERHOF, P OESPER"
+110,49SOR/DVO,,,,-,-,-,-,-,-,-,-
+111,50COR/VEL,,10.1016/0006-3002(50)90020-5,,-,-,-,-,-,-,-,-
+112,50FRI,15428423.0,10.1016/S0021-9258(19)50973-5,,['eng'],184,2,449-59,The Journal of biological chemistry,-,Jun 1950,M FRIEDMIN
+113,50HES,,10.1016/0006-3002(50)90037-0,,-,-,-,-,-,-,-,-
+114,50KOR,,10.1016/S0021-9258(18)56513-3,,-,-,-,-,-,-,-,-
+115,50OES/MEY,15419792.0,,,['eng'],27,1,223-33,Archives of biochemistry,-,Jun 1950,"P OESPER, O MEYERHOF"
+116,50PAZ,,,,-,-,-,-,-,-,-,-
+117,50RAC,15443900.0,10.1016/S0021-9258(19)51151-6,,['eng'],184,1,313-9,The Journal of biological chemistry,-,May 1950,E RACKER
+118,50SLE,14794671.0,10.1016/S0021-9258(18)56269-4,,['eng'],186,2,753-61,The Journal of biological chemistry,-,Oct 1950,M W SLEIN
+119,51BLA,14858331.0,10.1042/bj0490257,,['eng'],49,3,257-71,The Biochemical journal,-,Aug 1951,R L BLAKLEY
+120,51BLI,14830226.0,10.1016/0003-9861(51)90206-8,,['eng'],31,2,197-204,Archives of biochemistry and biophysics,-,Apr 1951,A F BLISS
+121,51FRU/JOH,14841149.0,10.1016/S0021-9258(18)56043-9,,['eng'],190,1,39-53,The Journal of biological chemistry,-,May 1951,"J S FRUTON, R B JOHNSTON, M FRIED"
+122,51KOR,,,,-,-,-,-,-,-,-,-
+123,51ROW/KOR,14907738.0,10.1016/S0021-9258(18)50905-4,,['eng'],193,2,497-507,The Journal of biological chemistry,-,Dec 1951,"J W ROWEN, A KORNBERG"
+124,51THE/BON,,10.3891/acta.chem.scand.05-1105,,-,-,-,-,-,-,-,-
+125,51WOO/GUN,14841188.0,10.1016/S0021-9258(18)56082-8,,['eng'],190,1,403-16,The Journal of biological chemistry,-,May 1951,"W A WOOD, I C GUNSALUS"
+126,52ASK,,,,-,-,-,-,-,-,-,-
+127,52BAU/GEM,14915545.0,10.1016/s0003-9861(52)80055-4,,['eng'],35,1,110-20,Archives of biochemistry and biophysics,-,Jan 1952,"C R BAUER, C L GEMMILL"
+128,52BUR,,10.1016/0006-3002(52)90020-6,,-,-,-,-,-,-,-,-
+129,52DOB/FRU,14938363.0,10.1016/S0021-9258(19)50883-3,,['eng'],195,1,149-54,The Journal of biological chemistry,-,Mar 1952,"A DOBRY, J S FRUTON, J M STURTEVANT"
+130,52DOB/STU,14938362.0,10.1016/S0021-9258(19)50882-1,,['eng'],195,1,141-7,The Journal of biological chemistry,-,Mar 1952,"A DOBRY, J M STURTEVANT"
+131,52EGG/HEM,13018181.0,10.1042/bj0520156,,['eng'],52,1,156-60,The Biochemical journal,-,Sep 1952,"L V EGGLESTON, R HEMS"
+132,52FIT/DOU,12999827.0,10.1016/S0021-9258(18)44822-3,,['eng'],199,1,153-63,The Journal of biological chemistry,-,Nov 1952,"C FITTING, M DOUDOROFF"
+133,52KOR,,,,-,-,-,-,-,-,-,-
+134,52LEL/CAR,,,,-,-,-,-,-,-,-,-
+135,52MEY/SHA,12997210.0,10.1016/0003-9861(52)90109-4,,['eng'],40,2,253-62,Archives of biochemistry and biophysics,-,Oct 1952,"O MEYERHOF, R SHATAS"
+136,52NAR/WOO,14924668.0,10.1016/s0003-9861(52)80026-8,,['eng'],35,2,462-3,Archives of biochemistry and biophysics,-,Feb 1952,"S A NARROD, W A WOOD"
+137,52NEI,12999850.0,10.1016/S0021-9258(18)44845-4,,['eng'],199,1,373-81,The Journal of biological chemistry,-,Nov 1952,J B NEILANDS
+138,52OHL/SHA,14944266.0,10.1016/0003-9861(52)90426-8,,['eng'],36,2,411-20,Archives of biochemistry and biophysics,-,Apr 1952,"P OHLMEYER, R SHATAS"
+139,52STA,12980996.0,10.1016/S0021-9258(19)52387-0,,['eng'],196,2,535-46,The Journal of biological chemistry,-,May 1952,E R STADTMAN
+140,52STE/OCH,12999746.0,10.1016/S0021-9258(18)55585-X,,['eng'],198,1,313-21,The Journal of biological chemistry,-,Sep 1952,"J R STERN, S OCHOA, F LYNEN"
+141,52STR/KOR,12981017.0,10.1016/S0021-9258(19)52408-5,,['eng'],196,2,769-84,The Journal of biological chemistry,-,May 1952,"H J STRECKER, S KORKES"
+142,53BOC/ALB,,10.1021/ja01104a043,,-,-,-,-,-,-,-,-
+143,53BOD,13061507.0,10.1016/S0021-9258(18)66196-4,,['eng'],202,2,829-40,The Journal of biological chemistry,-,Jun 1953,O BODANSKY
+144,53BRI,,10.3891/acta.chem.scand.07-1081,,-,-,-,-,-,-,-,-
+145,53BRO,13117866.0,10.1016/S0021-9258(18)66092-2,,['eng'],204,2,877-89,The Journal of biological chemistry,-,Oct 1953,D H BROWN
+146,53BUR/STA,13061511.0,10.1016/S0021-9258(18)66200-3,,['eng'],202,2,873-90,The Journal of biological chemistry,-,Jun 1953,"R M BURTON, E R STADTMAN"
+147,53BUR/WIL,13058837.0,10.1042/bj0540086,,['eng'],54,1,86-94,The Biochemical journal,-,Apr 1953,"K BURTON, T H WILSON"
+148,53COH,13044776.0,10.1016/S0021-9258(18)71349-5,,['eng'],201,1,71-84,The Journal of biological chemistry,-,Mar 1953,S COHEN
+149,53GRE/BRO,13117926.0,10.1016/S0021-9258(19)77273-1,,['eng'],205,1,493-501,The Journal of biological chemistry,-,Nov 1953,"I GREEN, J R BROWN, W F MOMMAERTS"
+150,53HAR/KOR,13084629.0,10.1016/S0021-9258(19)52329-8,,['eng'],203,2,595-604,The Journal of biological chemistry,-,Aug 1953,"I HARARY, S R KOREY, S OCHOA"
+151,53HOC/WAT,,10.1021/ja01109a516,,-,-,-,-,-,-,-,-
+152,53JON,13107745.0,,,['eng'],12,3,708-10,Federation proceedings,-,Sep 1953,M E JONES
+153,53KAP/COL,13117879.0,10.1016/S0021-9258(19)77226-3,,['eng'],205,1,1-15,The Journal of biological chemistry,-,Nov 1953,"N O KAPLAN, S P COLOWICK, E F NEUFELD"
+154,53KRE,13058835.0,10.1042/bj0540078,,['eng'],54,1,78-82,The Biochemical journal,-,Apr 1953,H A KREBS
+155,53KRE2,13058836.0,10.1042/bj0540082,,['eng'],54,1,82-6,The Biochemical journal,-,Apr 1953,H A KREBS
+156,53LYN/OCH,,10.1016/0006-3002(53)90149-8,,-,-,-,-,-,-,-,-
+157,53MAH/WAK,13084616.0,10.1016/S0021-9258(18)66153-8,,['eng'],204,1,453-68,The Journal of biological chemistry,-,Sep 1953,"H R MAHLER, S J WAKIL, R M BOCK"
+158,53MAS,13032036.0,10.1042/bj0530072,,['eng'],53,1,72-9,The Biochemical journal,-,Jan 1953,V MASSEY
+159,53MEY/SHA,,10.1016/0006-3002(53)90130-9,,-,-,-,-,-,-,-,-
+160,53MIT/LAM,13117877.0,10.1016/S0021-9258(18)66103-4,,['eng'],204,2,1011-8,The Journal of biological chemistry,-,Oct 1953,"S MITSUHASHI, J O LAMPEN"
+161,53NIS/BAR,13117873.0,10.1016/S0021-9258(18)66099-5,,['eng'],204,2,957-69,The Journal of biological chemistry,-,Oct 1953,"A NISONOFF, F W BARNES, T ENNS"
+162,53OLS/ANF,13061508.0,10.1016/S0021-9258(18)66197-6,,['eng'],202,2,841-56,The Journal of biological chemistry,-,Jun 1953,"J A OLSON, C B ANFINSEN"
+163,53RAT/ANS,13084582.0,10.1016/S0021-9258(18)66119-8,,['eng'],204,1,115-25,The Journal of biological chemistry,-,Sep 1953,"S RATNER, W P ANSLOW, B PETRACK"
+164,53SIE/POT,13034773.0,10.1016/S0021-9258(18)38451-5,,['eng'],200,1,187-96,The Journal of biological chemistry,-,Jan 1953,"P SIEKEVITZ, V R POTTER"
+165,53STE/COO,,10.1021/ja01102a540,,-,-,-,-,-,-,-,-
+166,53STR,13092953.0,10.1016/0003-9861(53)90176-3,,['eng'],46,1,128-40,Archives of biochemistry and biophysics,-,Sep 1953,H J STRECKER
+167,53STU,,10.1021/ja01104a527,,-,-,-,-,-,-,-,-
+168,53TAL/DOB,13129261.0,10.1016/S0021-9258(18)49226-5,,['eng'],205,2,823-37,The Journal of biological chemistry,-,Dec 1953,"P TALALAY, M M DOBSON"
+169,54AXE/JAN,13192139.0,10.1016/S0021-9258(18)65513-9,,['eng'],209,2,847-55,The Journal of biological chemistry,-,Aug 1954,"B AXELROD, R JANG"
+170,54BER/JOK,13211603.0,10.1016/S0021-9258(18)65392-X,,['eng'],210,2,657-72,The Journal of biological chemistry,-,Oct 1954,"P BERG, W K JOKLIK"
+171,54BOW/KER,13139680.0,10.1016/0003-9861(54)90176-9,,['eng'],49,1,149-59,Archives of biochemistry and biophysics,-,Mar 1954,"W J BOWEN, T D KERWIN"
+172,54CHA,13211661.0,10.1016/S0021-9258(18)71215-5,,['eng'],211,1,249-62,The Journal of biological chemistry,-,Nov 1954,F C CHARALAMPOUS
+173,54GIN,,,,-,-,-,-,-,-,-,-
+174,54GIN/STU,,10.1021/ja01637a015,,-,-,-,-,-,-,-,-
+175,54GOL,13174544.0,10.1016/S0021-9258(18)65653-4,,['eng'],208,1,345-57,The Journal of biological chemistry,-,May 1954,D S GOLDMAN
+176,54GRE/MII,13130521.0,10.1016/S0021-9258(18)71290-8,,['eng'],206,1,1-12,The Journal of biological chemistry,-,Jan 1954,"D E GREEN, S MII, H R MAHLER, R M BOCK"
+177,54HAN/CRA,13174537.0,10.1016/S0021-9258(18)65646-7,,['eng'],208,1,293-8,The Journal of biological chemistry,-,May 1954,"R G HANSEN, E M CRAINE"
+178,54HEL,13143026.0,10.1016/S0021-9258(19)50835-3,,['eng'],206,2,671-6,The Journal of biological chemistry,-,Feb 1954,P HELE
+179,54HOC/WAT,,10.1016/0003-9861(54)90313-6,,-,-,-,-,-,-,-,-
+180,54LEV/MEI,13192082.0,10.1016/S0021-9258(18)65554-1,,['eng'],209,1,265-80,The Journal of biological chemistry,-,Jul 1954,"L LEVINTOW, A MEISTER"
+181,54LIE/KOR,13163076.0,10.1016/S0021-9258(18)65708-4,,['eng'],207,2,911-24,The Journal of biological chemistry,-,Apr 1954,"I LIEBERMAN, A KORNBERG"
+182,54MAR/WIL,13159289.0,10.1016/0003-9861(54)90211-8,,['eng'],49,2,424-33,Archives of biochemistry and biophysics,-,Apr 1954,"A G MARR, P W WILSON"
+183,54MIT/DAV,,10.1016/0006-3002(54)90093-1,,-,-,-,-,-,-,-,-
+184,54NOD/KUB,,10.1016/S0021-9258(18)65434-1,,-,-,-,-,-,-,-,-
+185,54ROS/GRU,13221579.0,10.1016/S0021-9258(18)71161-7,,['eng'],211,2,737-56,The Journal of biological chemistry,-,Dec 1954,"I A ROSE, M GRUNBERG-MANAGO, S R KOREY, S OCHOA"
+186,54SIS/STA,13211620.0,10.1016/S0021-9258(18)65409-2,,['eng'],210,2,821-36,The Journal of biological chemistry,-,Oct 1954,"W R SISTROM, R Y STANIER"
+187,54STA,,,,-,-,-,-,-,-,-,-
+188,54STR/HAR,13211662.0,10.1016/S0021-9258(18)71216-7,,['eng'],211,1,263-70,The Journal of biological chemistry,-,Nov 1954,"H J STRECKER, I HARARY"
+189,54UTT/KUR,13163068.0,10.1016/S0021-9258(18)65700-X,,['eng'],207,2,821-41,The Journal of biological chemistry,-,Apr 1954,"M F UTTER, K KURAHASHI"
+190,54WAK/GRE,13163047.0,10.1016/S0021-9258(18)65679-0,,['eng'],207,2,631-8,The Journal of biological chemistry,-,Apr 1954,"S J WAKIL, D E GREEN, S MII, H R MAHLER"
+191,54WIL/BAN,13159356.0,10.1016/0003-9861(54)90072-7,,['eng'],50,2,513-5,Archives of biochemistry and biophysics,-,Jun 1954,"H G WILLIAMS-ASHMAN, J BANKS"
+192,55BLA/WRI,14353903.0,10.1016/S0021-9258(18)71041-7,,['eng'],213,1,27-38,The Journal of biological chemistry,-,Mar 1955,"S BLACK, N G WRIGHT"
+193,55BLA/WRI2,14353904.0,10.1016/S0021-9258(18)71042-9,,['eng'],213,1,39-50,The Journal of biological chemistry,-,Mar 1955,"S BLACK, N G WRIGHT"
+194,55BLA/WRI3,14353905.0,10.1016/S0021-9258(18)71043-0,,['eng'],213,1,51-60,The Journal of biological chemistry,-,Mar 1955,"S BLACK, N G WRIGHT"
+195,55BUC,,10.1016/0076-6879(55)01068-9,,-,-,-,-,-,-,-,-
+196,55BUR,,10.1016/0076-6879(55)01063-X,,-,-,-,-,-,-,-,-
+197,55CAR/COH,,10.1021/ja01607a095,,-,-,-,-,-,-,-,-
+198,55CAR/LEL,14367373.0,10.1016/S0021-9258(18)70953-8,,['eng'],214,1,149-55,The Journal of biological chemistry,-,May 1955,"C E CARDINI, L F LELOIR, J CHIRIBOGA"
+199,55DAV/GIL,,10.1016/S0076-6879(55)02203-9,,-,-,-,-,-,-,-,-
+200,55DEC,,,,-,-,-,-,-,-,-,-
+201,55DIC/WIL,,10.1038/176400a0,,-,-,-,-,-,-,-,-
+202,55GLA/BRO,13252007.0,10.1016/S0021-9258(19)52284-0,,['eng'],216,1,67-79,The Journal of biological chemistry,-,Sep 1955,"L GLASER, D H BROWN"
+203,55GRI/WAL,,10.1016/0006-3002(55)90122-0,,-,-,-,-,-,-,-,-
+204,55HOR/SMY,14353883.0,10.1016/S0021-9258(18)71020-X,,['eng'],212,2,811-25,The Journal of biological chemistry,-,Feb 1955,"B L HORECKER, P Z SMYRNIOTIS"
+205,55KAT,,10.1016/0006-3002(55)90353-X,,-,-,-,-,-,-,-,-
+206,55KAU/ALI,13252014.0,10.1016/S0021-9258(19)52291-8,,['eng'],216,1,141-52,The Journal of biological chemistry,-,Sep 1955,"S KAUFMAN, S G ALIVISATOS"
+207,55KIT/BEN,,10.1515/znb-1955-0704,,-,-,-,-,-,-,-,-
+208,55LEH/SIC,,10.1016/0006-3002(55)90368-1,,-,-,-,-,-,-,-,-
+209,55LIE/KOR,14392174.0,10.1016/S0021-9258(18)66048-X,,['eng'],215,1,403-51,The Journal of biological chemistry,-,Jul 1955,"I LIEBERMAN, A KORNBERG, E S SIMMS"
+210,55LIE/KOR2,14392176.0,10.1016/S0021-9258(18)66050-8,,['eng'],215,1,429-40,The Journal of biological chemistry,-,Jul 1955,"I LIEBERMAN, A KORNBERG, E S SIMMS"
+211,55LYN/WIE,,10.1016/0076-6879(55)01099-9,,-,-,-,-,-,-,-,-
+212,55MUN,,10.3891/acta.chem.scand.09-1523,,-,-,-,-,-,-,-,-
+213,55POD/STU,13271421.0,10.1016/S0021-9258(18)65925-3,,['eng'],217,2,603-6,The Journal of biological chemistry,-,Dec 1955,"R J PODOLSKY, J M STURTEVANT"
+214,55SLE,,10.1021/ja01611a074,,-,-,-,-,-,-,-,-
+215,55STA,,10.1016/0076-6879(55)01103-8,,-,-,-,-,-,-,-,-
+216,55STA/BUR,,10.1016/0076-6879(55)01089-6,,-,-,-,-,-,-,-,-
+217,55STU,,10.1021/ja01607a001,,-,-,-,-,-,-,-,-
+218,55STU2,,10.1021/ja01611a026,,-,-,-,-,-,-,-,-
+219,55THO/GOM,14367287.0,10.1128/jb.69.3.357-362.1955,,['eng'],69,3,357-62,Journal of bacteriology,-,Mar 1955,"C B THORNE, C G GOMEZ, R D HOUSEWRIGHT"
+220,55VAR/WEB,16654798.0,10.1104/pp.30.5.393,,['eng'],30,5,393-402,Plant physiology,-,Sep 1955,"J E Varner, G C Webster"
+221,55WIL/MCI,13271408.0,10.1016/S0021-9258(19)57195-2,,['eng'],217,1,467-77,The Journal of biological chemistry,-,Nov 1955,"V R WILLIAMS, R T MCINTYRE"
+222,55WOL/KAP,,10.1016/0076-6879(55)01050-1,,-,-,-,-,-,-,-,-
+223,55YAN/GIL,14367339.0,10.1016/S0021-9258(18)98210-4,,['eng'],213,2,787-95,The Journal of biological chemistry,-,Apr 1955,"H YANIV, C GILVARG"
+224,55ZEL,13271335.0,10.1016/S0021-9258(19)81413-8,,['eng'],216,2,553-75,The Journal of biological chemistry,-,Oct 1955,I ZELITCH
+225,56ALE/GRE,13331936.0,10.1016/S0021-9258(18)65303-7,,['eng'],220,2,775-85,The Journal of biological chemistry,-,Jun 1956,"N ALEXANDER, D M GREENBERG"
+226,56AME/HOR,13319331.0,10.1016/S0021-9258(18)65337-2,,['eng'],220,1,113-28,The Journal of biological chemistry,-,May 1956,"B N AMES, B L HORECKER"
+227,56BEN/HEM,16589970.0,10.1073/pnas.42.12.896,,['eng'],42,12,896-900,Proceedings of the National Academy of Sciences of the United States of America,-,Dec 1956,"T H Benzinger, R Hems"
+228,56BOW/KER,13363434.0,10.1016/0003-9861(56)90270-3,,['eng'],64,2,278-84,Archives of biochemistry and biophysics,-,Oct 1956,"W J BOWEN, T D KERWIN"
+229,56CAR/COH,13366975.0,10.1016/S0021-9258(19)50767-0,,['eng'],222,1,17-30,The Journal of biological chemistry,-,Sep 1956,"C E CARTER, L H COHEN"
+230,56COW/PIZ,13385236.0,10.1016/S0021-9258(18)65087-2,,['eng'],223,2,885-95,The Journal of biological chemistry,-,Dec 1956,"R W COWGILL, L I PIZER"
+231,56DIC/WIL,13373810.0,10.1042/bj0640567,,['eng'],64,3,567-78,The Biochemical journal,-,Nov 1956,"F DICKENS, D H WILLIAMSON"
+232,56ENG,,,,-,-,-,-,-,-,-,-
+233,56FEU/WOL,13354402.0,,,['ger'],10,1,1-10,Acta physiologica Academiae Scientiarum Hungaricae,-, 1956,"G FEUER, M WOLLEMANN"
+234,56FOR/GUT,,10.1021/ja01588a024,,-,-,-,-,-,-,-,-
+235,56GRE/COH,13319278.0,10.1016/S0021-9258(18)65716-3,,['eng'],219,2,557-68,The Journal of biological chemistry,-,Apr 1956,"M GREEN, S S COHEN"
+236,56HAK/GLA,13345810.0,10.1016/S0021-9258(18)65240-8,,['eng'],221,1,191-209,The Journal of biological chemistry,-,Jul 1956,"M T HAKALA, A J GLAID, G W SCHWERT"
+237,56HAU,,10.1021/ja01601a032,,-,-,-,-,-,-,-,-
+238,56HUB,,10.1085/jgp.39.6.935,,-,-,-,-,-,-,-,-
+239,56HUR/HOR,13385247.0,10.1016/S0021-9258(18)65098-7,,['eng'],223,2,993-1008,The Journal of biological chemistry,-,Dec 1956,"B L HORECKER, J HURWITZ"
+240,56KAP/CIO,13357478.0,10.1016/S0021-9258(18)65197-X,,['eng'],221,2,833-44,The Journal of biological chemistry,-,Aug 1956,"M M CIOTTI, N O KAPLAN, F E STOLZENBACH"
+241,56KIT/HOR,,,,-,-,-,-,-,-,-,-
+242,56LAR/JAC,13292912.0,10.1016/0003-9861(56)90437-4,,['eng'],60,2,352-63,Archives of biochemistry and biophysics,-,Feb 1956,"J LARNER, W T JACKSON, D J GRAVES, J R STAMER"
+243,56LEL/CAR,,10.1016/0006-3002(56)90259-1,,-,-,-,-,-,-,-,-
+244,56PAL/DOU,13278359.0,10.1016/S0021-9258(18)65915-0,,['eng'],218,1,535-48,The Journal of biological chemistry,-,Jan 1956,"N J PALLERONI, M DOUDOROFF"
+245,56POD/MOR,13295245.0,10.1016/S0021-9258(18)65857-0,,['eng'],218,2,945-59,The Journal of biological chemistry,-,Feb 1956,"R J PODOLSKY, M F MORALES"
+246,56RAB/PRI,,10.1021/ja01597a094,,-,-,-,-,-,-,-,-
+247,56RAM/GIR,13314642.0,10.1016/0003-9861(56)90091-1,,['eng'],62,1,91-6,Archives of biochemistry and biophysics,-,May 1956,"T RAMASARMA, K V GIRI"
+248,56RAT/ROC,13355454.0,10.1016/0003-9861(56)90044-3,,['eng'],63,2,277-95,Archives of biochemistry and biophysics,-,Aug 1956,"S RATNER, O ROCHOVANSKY"
+249,56REI,13319297.0,10.1016/S0021-9258(18)65735-7,,['eng'],219,2,753-67,The Journal of biological chemistry,-,Apr 1956,J L REISSIG
+250,56SMI/STA,,10.1016/0006-3002(56)90493-0,,-,-,-,-,-,-,-,-
+251,56STE,13345796.0,10.1016/S0021-9258(18)65226-3,,['eng'],221,1,33-44,The Journal of biological chemistry,-,Jul 1956,J R STERN
+252,56STE/COO,13345795.0,10.1016/S0021-9258(18)65225-1,,['eng'],221,1,15-31,The Journal of biological chemistry,-,Jul 1956,"J R STERN, M J COON, A DEL CAMPILLO, M C SCHNEIDER"
+253,56STE/DEL,13295248.0,10.1016/S0021-9258(18)65860-0,,['eng'],218,2,985-1002,The Journal of biological chemistry,-,Feb 1956,"J R STERN, A DEL CAMPILLO"
+254,56STU/HOR,13295228.0,10.1016/S0021-9258(18)65840-5,,['eng'],218,2,753-68,The Journal of biological chemistry,-,Feb 1956,"P K STUMPF, B L HORECKER"
+255,56TAL/MAR,13295222.0,10.1016/S0021-9258(18)65834-X,,['eng'],218,2,675-91,The Journal of biological chemistry,-,Feb 1956,"P TALALAY, P I MARCUS"
+256,56TOM,13278351.0,10.1016/S0021-9258(18)65907-1,,['eng'],218,1,437-47,The Journal of biological chemistry,-,Jan 1956,G M TOMKINS
+257,56WOL/KAP,13295236.0,10.1016/S0021-9258(18)65848-X,,['eng'],218,2,849-69,The Journal of biological chemistry,-,Feb 1956,"J B WOLFF, N O KAPLAN"
+258,57ASH/HIC,13428737.0,10.1016/S0021-9258(18)64805-7,,['eng'],226,1,65-76,The Journal of biological chemistry,-,May 1957,"G ASHWELL, J HICKMAN"
+259,57BUR/HOR,,10.1016/0006-3002(57)90272-X,,-,-,-,-,-,-,-,-
+260,57CAL,13488919.0,10.1042/bj0670651,,['eng'],67,4,651-7,The Biochemical journal,-,Dec 1957,O H CALLAGHAN
+261,57DOU/CON,,,,-,-,-,-,-,-,-,-
+262,57DUR/STU,,10.1016/0006-3002(57)90006-9,,-,-,-,-,-,-,-,-
+263,57FLA/ERW,13475309.0,10.1016/S0021-9258(18)70703-5,,['eng'],228,1,201-13,The Journal of biological chemistry,-,Sep 1957,"J G FLAKS, M J ERWIN, J M BUCHANAN"
+264,57GRE/LIP,13502367.0,10.1016/S0021-9258(19)63710-5,,['eng'],229,2,1081-90,The Journal of biological chemistry,-,Dec 1957,"J D GREGORY, F LIPMANN"
+265,57HOH,13426146.0,,,['ger'],328,7,509-21,Biochemische Zeitschrift,-, 1957,H J HOHORST
+266,57HOL/HOL,13522707.0,,,['ger'],329,4,292-312,Biochemische Zeitschrift,-, 1957,"H HOLZER, A HOLLDORF"
+267,57HOL/TOU,13416220.0,10.1016/S0021-9258(18)64912-9,,['eng'],225,1,87-102,The Journal of biological chemistry,-,Mar 1957,"S HOLLMANN, O TOUSTER"
+268,57KAR/GRE,13449064.0,10.1016/S0021-9258(18)70806-5,,['eng'],227,1,191-205,The Journal of biological chemistry,-,Jul 1957,"M A KARASEK, D M GREENBERG"
+269,57MAX,13491567.0,10.1016/S0021-9258(18)70602-9,,['eng'],229,1,139-51,The Journal of biological chemistry,-,Nov 1957,E S MAXWELL
+270,57REI,,10.3891/acta.chem.scand.11-0523,,-,-,-,-,-,-,-,-
+271,57ROB/BOY,13398392.0,10.1016/S0021-9258(18)65015-X,,['eng'],224,1,121-35,The Journal of biological chemistry,-,Jan 1957,"P D BOYER, E A ROBBINS"
+272,57ROB/COO,13416257.0,10.1016/S0021-9258(18)64948-8,,['eng'],225,1,511-21,The Journal of biological chemistry,-,Mar 1957,"W G ROBINSON, M J COON"
+273,57ROD/TOW,13475367.0,10.1016/S0021-9258(18)70667-4,,['eng'],228,2,875-90,The Journal of biological chemistry,-,Oct 1957,"V W RODWELL, J C TOWNE, S GRISOLIA"
+274,57SAN/SEA,,10.1016/0006-3002(57)90179-8,,-,-,-,-,-,-,-,-
+275,57SMI/GUN,13491582.0,10.1016/S0021-9258(18)70617-0,,['eng'],229,1,305-19,The Journal of biological chemistry,-,Nov 1957,"R A SMITH, I C GUNSALUS"
+276,57STE,,10.1016/0006-3002(57)90040-9,,-,-,-,-,-,-,-,-
+277,57TAL,,,,-,-,-,-,-,-,-,-
+278,57VLA/VLA,13499474.0,,,['rus'],22,6,963-70,"Biokhimiia (Moscow, Russia)",-, 1957,"G E VLADIMIROV, V G VLASOVA, A I KOLOTILOVA, S N LYZLOVA, N S PANTELEEVA"
+279,57VLA/VLA2,13451618.0,10.1038/1791350a0,,['eng'],179,4574,1350-1,Nature,-,Jun 1957,"G E VLADIMIROV, V G VLASSOVA, A Y KOLOTILOVA, S N LYZLOVA, N S PANTELEYEVA"
+280,57WOL/BAL,,10.1016/S0021-9258(18)70816-8,,-,-,-,-,-,-,-,-
+281,58BAC,,10.3891/acta.chem.scand.12-1279,,-,-,-,-,-,-,-,-
+282,58BRU/NOL,13596391.0,,,['ger'],330,6,483-96,Biochemische Zeitschrift,-, 1958,"F H BRUNS, E NOLTMANN, E VAHLHAUS"
+283,58BUR/HOR,13539036.0,10.1016/S0021-9258(18)70466-3,,['eng'],231,2,1053-64,The Journal of biological chemistry,-,Apr 1958,"D P BURMA, B L HORECKER"
+284,58CAB/LEL,13538966.0,10.1016/S0021-9258(19)77303-7,,['eng'],231,1,259-75,The Journal of biological chemistry,-,Mar 1958,"E CABIB, L F LELOIR"
+285,58FRO,,10.1016/0006-3002(58)90182-3,,-,-,-,-,-,-,-,-
+286,58FRO2,13598730.0,10.1016/S0021-9258(19)77337-2,,['eng'],233,5,1049-52,The Journal of biological chemistry,-,Nov 1958,H J FROMM
+287,58HEA/HOR,13539034.0,10.1016/S0021-9258(18)70464-X,,['eng'],231,2,1031-7,The Journal of biological chemistry,-,Apr 1958,"E C HEATH, B L HORECKER, P Z SMYRNIOTIS, Y TAKAGI"
+288,58LAN/ENG,13575417.0,10.1016/S0021-9258(18)64708-8,,['eng'],233,3,583-8,The Journal of biological chemistry,-,Sep 1958,"L J LANGER, L L ENGEL"
+289,58MAL/OCH,13610869.0,10.1016/S0021-9258(18)49368-4,,['eng'],233,6,1538-43,The Journal of biological chemistry,-,Dec 1958,"F MALEY, S OCHOA"
+290,58MCQ,,,appears in part 2,-,-,-,-,-,-,-,-
+291,58NOL/BRU,13596394.0,,,['ger'],330,6,514-20,Biochemische Zeitschrift,-, 1958,"E NOLTMANN, F H BRUNS"
+292,58ROB/LIP,13575437.0,10.1016/S0021-9258(18)64728-3,,['eng'],233,3,686-90,The Journal of biological chemistry,-,Sep 1958,"P W ROBBINS, F LIPMANN"
+293,58TAB/SRE,13534662.0,10.1016/0003-9861(58)90003-1,,['eng'],74,2,315-25,Archives of biochemistry and biophysics,-,Apr 1958,"M TABACHNICK, P A SRERE, J COOPER, E RACKER"
+294,58TUR/TUR,13560389.0,10.1042/bj0690448,,['eng'],69,3,448-52,The Biochemical journal,-,Jul 1958,"D H TURNER, J F TURNER"
+295,58WIL/BAN,13587526.0,10.1016/S0021-9258(18)64689-7,,['eng'],233,4,975-81,The Journal of biological chemistry,-,Oct 1958,"L G WILSON, R S BANDURSKI"
+296,58WOL/SIM,13549442.0,10.1016/S0021-9258(18)70419-5,,"['eng', 'rus']",232,1,559-75,The Journal of biological chemistry,-,May 1958,"M J WOLIN, F J SIMPSON, W A WOOD"
+297,58YOU/PAC,13534693.0,10.1016/0003-9861(58)90403-x,,['eng'],75,1,125-41,Archives of biochemistry and biophysics,-,May 1958,"H L YOUNG, N PACE"
+298,59ALE,,,,-,-,-,-,-,-,-,-
+299,59ATK/JOH,,10.1038/1841925a0,,-,-,-,-,-,-,-,-
+300,59BAR/SMY,13630903.0,10.1016/S0021-9258(18)70297-4,,['eng'],234,2,320-8,The Journal of biological chemistry,-,Feb 1959,"H A BARKER, R D SMYTH, R M WILSON, H WEISSBACH"
+301,59BEN/KIT,13628584.0,10.1042/bj0710400,,['eng'],71,2,400-7,The Biochemical journal,-,Feb 1959,"T BENZINGER, C KITZINGER, R HEMS, K BURTON"
+302,59BON/PON,,10.1016/0006-291X(59)90066-X,,-,-,-,-,-,-,-,-
+303,59CAL/WEB,13806976.0,10.1042/bj0730473,,['eng'],73,3,473-85,The Biochemical journal,-,Nov 1959,"O H CALLAGHAN, G WEBER"
+304,59CHI/SUG,,10.1080/03758397.1959.10857560,,-,-,-,-,-,-,-,-
+305,59DEL/DEF,,10.1016/0006-3002(59)90495-0,,-,-,-,-,-,-,-,-
+306,59DEN/ROB,13672942.0,10.1016/S0021-9258(18)69904-1,,['eng'],234,7,1666-71,The Journal of biological chemistry,-,Jul 1959,"H DEN, W G ROBINSON, M J COON"
+307,59FRI,13825045.0,10.1016/S0021-9258(18)69689-9,,['eng'],234,-,2891-6,The Journal of biological chemistry,-,Nov 1959,C FRIEDEN
+308,59GOL,,10.1016/0006-3002(59)90555-4,,-,-,-,-,-,-,-,-
+309,59HAB/CAN,13641268.0,10.1016/S0021-9258(18)70253-6,,['eng'],234,3,603-8,The Journal of biological chemistry,-,Mar 1959,"G DE LA HABA, G L CANTONI"
+310,59HOL,14402710.0,10.1515/bchm2.1959.317.1.193,,['ger'],317,-,193-216,Hoppe-Seyler's Zeitschrift fur physiologische Chemie,-, 1959,S HOLLMANN
+311,59ITO/GRI,13630886.0,10.1016/S0021-9258(18)70280-9,,['eng'],234,2,242-5,The Journal of biological chemistry,-,Feb 1959,"N ITO, S GRISOLIA"
+312,59KIR/TUR,14409347.0,10.1042/bj0720716,,['eng'],72,4,716-20,The Biochemical journal,-,Aug 1959,"R J KIRKLAND, J F TURNER"
+313,59KIT/HEM,13628583.0,10.1042/bj0710395,,['eng'],71,2,395-400,The Biochemical journal,-,Feb 1959,"C KITZINGER, R HEMS"
+314,59KRI,13630884.0,10.1016/S0021-9258(18)70278-0,,['eng'],234,2,232-6,The Journal of biological chemistry,-,Feb 1959,I KRIMSKY
+315,59MCC/NAJ,,10.1016/S0021-9258(18)69716-9,,-,-,-,-,-,-,-,-
+316,59MCQ/UTT,13673030.0,10.1016/S0021-9258(18)69883-7,,['eng'],234,8,2151-7,The Journal of biological chemistry,-,Aug 1959,"J T McQUATE, M F UTTER"
+317,59MER/TOM,,10.1016/S0021-9258(18)69780-7,,-,-,-,-,-,-,-,-
+318,59MIL/LUK,13672968.0,10.1016/S0021-9258(18)69930-2,,['eng'],234,7,1806-11,The Journal of biological chemistry,-,Jul 1959,"R W MILLER, L N LUKENS, J M BUCHANAN"
+319,59NOR/FRO,14427582.0,10.1016/S0021-9258(18)69732-7,,['eng'],234,-,2523-31,The Journal of biological chemistry,-,Oct 1959,"R C NORDLIE, H J FROMM"
+320,59SAN/LAN,13610916.0,10.1016/S0021-9258(18)70359-1,,['eng'],234,1,178-82,The Journal of biological chemistry,-,Jan 1959,"D R SANADI, M LANGLEY, R L SEARLS"
+321,59SCO/JAK,13654294.0,10.1016/S0021-9258(18)70206-8,,['eng'],234,4,932-6,The Journal of biological chemistry,-,Apr 1959,"E M SCOTT, W B JAKOBY"
+322,59SHO/PRI,13664648.0,10.1128/jb.77.6.695-700.1959,,['eng'],77,6,695-700,Journal of bacteriology,-,Jun 1959,"T E SHOCKLEY, H S PRIDE"
+323,59STR/SMI,13672971.0,10.1016/S0021-9258(18)69933-8,,['eng'],234,7,1822-7,The Journal of biological chemistry,-,Jul 1959,"J L STROMINGER, M S SMITH"
+324,59TAB/WYN,13672973.0,10.1016/S0021-9258(18)69935-1,,['eng'],234,7,1830-46,The Journal of biological chemistry,-,Jul 1959,"H TABOR, L WYNGARDEN"
+325,59TAL/LEV,,,,-,-,-,-,-,-,-,-
+326,59VAG/EAR,13641247.0,10.1016/S0021-9258(18)70232-9,,['eng'],234,3,490-7,The Journal of biological chemistry,-,Mar 1959,"P R VAGELOS, J M EARL, E R STADTMAN"
+327,60AGO/ARA,13681649.0,,,['eng'],22,-,281-94,Enzymologia,-,Dec 1960,"M AGOSIN, L ARAVENA"
+328,60ASH/WAH,13794771.0,10.1016/S0021-9258(19)76840-9,,['eng'],235,-,1559-65,The Journal of biological chemistry,-,Jun 1960,"G ASHWELL, A J WAHBA, J HICKMAN"
+329,60BLA,13801272.0,10.1042/bj0740071,,['eng'],74,1,71-82,The Biochemical journal,-,Jan 1960,R L BLAKLEY
+330,60COM/ROS,13811398.0,10.1016/S0021-9258(19)76908-7,,['eng'],235,-,2529-37,The Journal of biological chemistry,-,Sep 1960,"D G COMB, S ROSEMAN"
+331,60FEI/NEU,13821949.0,10.1016/S0021-9258(18)69449-9,,['eng'],235,-,910-3,The Journal of biological chemistry,-,Apr 1960,"D S FEINGOLD, E F NEUFELD, W Z HASSID"
+332,60GEL/STU,,10.1021/ja01491a053,,-,-,-,-,-,-,-,-
+333,60GUP/ROB,13830319.0,10.1016/S0021-9258(19)76849-5,,['eng'],235,-,1609-12,The Journal of biological chemistry,-,Jun 1960,"N K GUPTA, W G ROBINSON"
+334,60ICH/FUR,,10.1093/oxfordjournals.jbchem.a127169,,-,-,-,-,-,-,-,-
+335,60ISH,,,,-,-,-,-,-,-,-,-
+336,60JON/LIP,16590733.0,10.1073/pnas.46.9.1194,,['eng'],46,9,1194-205,Proceedings of the National Academy of Sciences of the United States of America,-,Sep 1960,"M E Jones, F Lipmann"
+337,60KAH/LOW,14408402.0,10.1016/S0021-9258(18)64594-6,,['eng'],235,-,2178-84,The Journal of biological chemistry,-,Aug 1960,"S E KAHANA, O H LOWRY, D W SCHULZ, J V PASSONNEAU, E J CRAWFORD"
+338,60KAY/OSB,14404999.0,10.1016/S0021-9258(18)69609-7,,['eng'],235,-,195-201,The Journal of biological chemistry,-,Jan 1960,"L D KAY, M J OSBORN, Y HATEFI, F M HUENNEKENS"
+339,60KUR/SUG,14412847.0,10.1016/S0021-9258(18)69456-6,,['eng'],235,-,940-6,The Journal of biological chemistry,-,Apr 1960,"K KURAHASHI, A SUGIMURA"
+340,60LEA/GLA,13759914.0,10.1016/S0021-9258(20)81338-6,,['eng'],235,-,3209-12,The Journal of biological chemistry,-,Nov 1960,"J LEAHY, E GLASSMAN, R S SCHWEET"
+341,60MAX/ROB,,10.1016/S0021-9258(18)69520-1,,-,-,-,-,-,-,-,-
+342,60MEN,13769376.0,10.1016/S0021-9258(18)64469-2,,['eng'],235,-,3347-52,The Journal of biological chemistry,-,Dec 1960,J MENDICINO
+343,60NIR/JAK,14427301.0,10.1016/S0021-9258(18)69459-1,,['eng'],235,-,954-60,The Journal of biological chemistry,-,Apr 1960,"M W NIRENBERG, W B JAKOBY"
+344,60OCO/HAL,13730045.0,10.1016/0003-9861(60)90503-8,,['eng'],91,-,290-9,Archives of biochemistry and biophysics,-,Dec 1960,"R J O'CONNOR, H O HALVORSON"
+345,60PIE/WIA,,10.1016/0006-3002(60)90506-0,,-,-,-,-,-,-,-,-
+346,60PRI/HOR,14434864.0,10.1016/S0021-9258(18)69401-3,,['eng'],235,-,1292-8,The Journal of biological chemistry,-,May 1960,"W E PRICER, B L HORECKER"
+347,60SCH/RAT,13748745.0,10.1016/S0021-9258(18)64515-6,,['eng'],235,-,3597-602,The Journal of biological chemistry,-,Dec 1960,"A SCHUEGRAF, S RATNER, R C WARNER"
+348,60VOL,,10.1016/S0021-9258(19)76838-0,,-,-,-,-,-,-,-,-
+349,61ALE,13682344.0,10.1128/jb.81.6.903-910.1961,,['eng'],81,6,903-10,Journal of bacteriology,-,Jun 1961,J K ALEXANDER
+350,61ATK/BUR,13684980.0,10.1042/bj0780813,,['eng'],78,4,813-20,The Biochemical journal,-,Apr 1961,"M R ATKINSON, R M BURTON, R K MORTON"
+351,61ATK/JOH,13684982.0,10.1042/bj0790012,,['eng'],79,1,12-5,The Biochemical journal,-,Apr 1961,"M R ATKINSON, E JOHNSON, R K MORTON"
+352,61BEN/SCH,,10.1016/S0021-9258(18)64053-0,,-,-,-,-,-,-,-,-
+353,61BER/BER,,10.1016/S0021-9258(19)63293-X,,-,-,-,-,-,-,-,-
+354,61CAN,,,,-,-,-,-,-,-,-,-
+355,61DAT/RAC,13719876.0,10.1016/S0021-9258(18)64277-2,,['eng'],236,-,617-23,The Journal of biological chemistry,-,Mar 1961,"A G DATTA, E RACKER"
+356,61DOU,,,,-,-,-,-,-,-,-,-
+357,61DOU/MER,,,,-,-,-,-,-,-,-,-
+358,61GAW/GLA,13897360.0,10.1016/0003-9861(61)90136-9,,['eng'],95,-,203-10,Archives of biochemistry and biophysics,-,Nov 1961,"O GAWRON, A J GLAID, R E BOYLE, G ODSTRCHEL"
+359,61GOT/KOR,13900766.0,10.1042/bj0810273,,['eng'],81,2,273-84,The Biochemical journal,-,Nov 1961,"A M GOTTO, H L KORNBERG"
+360,61KLE,,,,-,-,-,-,-,-,-,-
+361,61KOR/GLA,13753209.0,10.1016/S0021-9258(19)63304-1,,['eng'],236,-,1791-4,The Journal of biological chemistry,-,Jun 1961,"S KORNFELD, L GLASER"
+362,61KRA/VEN,13753903.0,10.1016/S0021-9258(18)64442-4,,['eng'],236,-,142-4,The Journal of biological chemistry,-,Jan 1961,"G KRAKOW, B VENNESLAND"
+363,61LED,14463407.0,10.1016/S0021-9258(19)76430-8,,['eng'],236,-,3066-71,The Journal of biological chemistry,-,Nov 1961,I G LEDER
+364,61MAH,,,,-,-,-,-,-,-,-,-
+365,61PRA,,,,-,-,-,-,-,-,-,-
+366,61RAC,,,,-,-,-,-,-,-,-,-
+367,61RAC2,,,,-,-,-,-,-,-,-,-
+368,61RAW/WAD,,10.1021/ja01476a003,,-,-,-,-,-,-,-,-
+369,61SAN/ZIN,13746411.0,10.1016/0003-9861(61)90070-4,,['eng'],94,-,430-5,Archives of biochemistry and biophysics,-,Sep 1961,"B D SANWAL, M W ZINK"
+370,61VEN/RAC,13780711.0,10.1016/S0021-9258(18)64098-0,,['eng'],236,-,1876-82,The Journal of biological chemistry,-,Jul 1961,"R VENKATARAMAN, E RACKER"
+371,61VLA/KOM,13781723.0,,,['rus'],26,-,426-30,"Biokhimiia (Moscow, Russia)",-, 1961,"G E VLADIMIROVA, A I KOMKOVA, N A FEDOROVA"
+372,61WIL/WIL,13785328.0,10.1016/0003-9861(61)90318-6,,['eng'],93,-,80-4,Archives of biochemistry and biophysics,-,Apr 1961,"J S WILKINSON, V R WILLIAMS"
+373,61WOO/STJ,13786500.0,10.1073/pnas.47.3.289,,['eng'],47,3,289-303,Proceedings of the National Academy of Sciences of the United States of America,-,Mar 1961,"H G WOOD, R STJERNHOLM"
+374,61YAM,14008731.0,10.1016/S0021-9258(19)76425-4,,['eng'],236,-,3043-6,The Journal of biological chemistry,-,Nov 1961,E W YAMADA
+375,62AKA/CAM,16561978.0,10.1128/jb.84.6.1194-1201.1962,,['eng'],84,6,1194-201,Journal of bacteriology,"Akagi, J. M. (University of Kansas, Lawrence) and L. Leon Campbell. Studies on thermophilic sulfate-reducing bacteria. III. Adenosine triphosphate-sulfurylase of Clostridium nigrificans and Desulfovibrio desulfuricans. J. Bacteriol. 84:1194-1201. 1962.-Adenosine triphosphate (ATP)-sulfurylase, which catalyzes the formation of adenosine-5'-phosphosulfate (APS) from ATP and SO(4) (=), has been purified from crude extracts of Clostridium nigrificans and Desulfovibrio desulfuricans by (NH(4))(2)SO(4) fractionation and triethylaminoethyl column chromatography. The enzyme from both sources operates over a broad pH range from 6.0 to 9.5. Below pH 6.0, activity decreases sharply, with no detectable activity at pH 5.0. Of the nucleotides tested (ATP and the triphosphates of deoxyadenosine, uridine, inosine, and guanosine), only ATP was acted upon by the enzyme from either source. The enzyme requires Mg(++) for activity. Incubation of the enzyme from both organisms with ATP and S(35)O(4) (=) in the presence of helium resulted in the formation of an S(35)-labeled nucleotide whose electrophoretic mobility was identical to that of chemically prepared APS. When incubated with ATP and the group VI anions (CrO(4), MoO(4), WO(4)), the enzyme from both organisms formed an unstable intermediate, resulting in the accumulation of pyrophosphate. Thermal stability studies revealed that the ATP-sulfurylase of C. nigrificans was stable at higher temperatures than the enzyme obtained from D. desulfuricans. Exposure of the enzyme from C. nigrificans to 65 C for 2 hr gave virtually no decrease in activity. In contrast, the enzyme from D. desulfuricans was completely inactivated after 30 min at 55 C, after 3 min at 60 C, or after 1 min at 65 C.",Dec 1962,"J M Akagi, L L Campbell"
+376,62BES,,10.1016/0076-6879(63)06160-7,,-,-,-,-,-,-,-,-
+377,62BLA,,10.1016/S0076-6879(62)05320-3,,-,-,-,-,-,-,-,-
+378,62BRU/JOU,13874013.0,10.1016/S0021-9258(19)73772-7,,['eng'],237,-,2447-53,The Journal of biological chemistry,-,Aug 1962,"P BRUNETTI, G W JOURDIAN, S ROSEMAN"
+379,62CHA/VEI,13877918.0,10.1016/S0021-9258(18)60275-3,,['eng'],237,-,1014-20,The Journal of biological chemistry,-,Apr 1962,"M CHAKRAVORTY, L A VEIGA, M BACILA, B L HORECKER"
+380,62COM/ROS,,10.1016/S0076-6879(62)05246-5,appears in part 6,-,-,-,-,-,-,-,-
+381,62DOU/SHU,,,,-,-,-,-,-,-,-,-
+382,62DOU2,,10.1016/S0076-6879(62)05234-9,,-,-,-,-,-,-,-,-
+383,62DUR/RAW,,10.1016/0006-3002(62)90607-8,,-,-,-,-,-,-,-,-
+384,62ESP,,10.1016/S0021-9258(19)84491-5,,-,-,-,-,-,-,-,-
+385,62GHA/HEA,13898172.0,10.1016/S0021-9258(19)73768-5,,['eng'],237,-,2427-33,The Journal of biological chemistry,-,Aug 1962,"M A GHALAMBOR, E C HEATH"
+386,62GOL/WAG,,10.1016/0006-3002(62)91048-X,,-,-,-,-,-,-,-,-
+387,62GRI,,10.1016/S0076-6879(62)05210-6,,-,-,-,-,-,-,-,-
+388,62HAL/FEN,13903809.0,10.1016/S0021-9258(19)63410-1,,['eng'],237,-,2140-7,The Journal of biological chemistry,-,Jul 1962,"D R HALENZ, J Y FENG, C S HEGRE, M D LANE"
+389,62HAY/NIS,,10.1016/S0076-6879(62)05297-0,,-,-,-,-,-,-,-,-
+390,62HIM/RAB,13907490.0,10.1016/S0021-9258(18)60249-2,,['eng'],237,-,2903-14,The Journal of biological chemistry,-,Sep 1962,"R H HIMES, J C RABINOWITZ"
+391,62HOR,,10.1016/S0076-6879(62)05212-X,,-,-,-,-,-,-,-,-
+392,62JAK,,10.1016/S0076-6879(62)05311-2,,-,-,-,-,-,-,-,-
+393,62KRE/MEL,14459507.0,10.1042/bj0820096,,['eng'],82,1,96-8,The Biochemical journal,-,Jan 1962,"H A KREBS, J MELLANBY, D H WILLIAMSON"
+394,62MEN,14472566.0,10.1016/S0021-9258(18)81380-1,,['eng'],237,-,165-9,The Journal of biological chemistry,-,Jan 1962,J MENDICINO
+395,62PET,,10.1016/S0076-6879(62)05327-6,,-,-,-,-,-,-,-,-
+396,62RAB,,,should this be 62RAZ? appears in part 2,-,-,-,-,-,-,-,-
+397,62RAT,,10.1016/S0076-6879(62)05324-0,should this be 62RAB? appears in part 2,-,-,-,-,-,-,-,-
+398,62RAV/WOL,14490617.0,10.1021/bi00908a012,,['eng'],1,-,263-9,Biochemistry,-,Mar 1962,"D N RAVAL, R G WOLFE"
+399,62RAV/WOL2,,10.1021/bi00912a023,,-,-,-,-,-,-,-,-
+400,62SEG/BEA,,10.1016/S0021-9258(19)73958-1,,-,-,-,-,-,-,-,-
+401,62SHU/DOU,13912428.0,10.1016/S0021-9258(18)93969-4,,['eng'],237,-,603-7,The Journal of biological chemistry,-,Feb 1962,"C W SHUSTER, M DOUDOROFF"
+402,62SIL,,10.1016/S0076-6879(62)05314-8,,-,-,-,-,-,-,-,-
+403,62TAB,,10.1016/S0076-6879(62)05313-6,appears in part 2,-,-,-,-,-,-,-,-
+404,62UEH,,10.1016/S0076-6879(62)05238-6,,-,-,-,-,-,-,-,-
+405,62WIL/SNE,14001018.0,10.1016/S0021-9258(18)50139-3,,['eng'],237,-,3171-9,The Journal of biological chemistry,-,Oct 1962,"E M WILSON, E E SNELL"
+406,63ALL/KEL,14012144.0,10.1016/S0021-9258(18)81114-0,,['eng'],238,-,1637-42,The Journal of biological chemistry,-,May 1963,"S H ALLEN, R KELLERMEYER, R STJERNHOLM, B JACOBSON, H G WOOD"
+407,63BEC/LEV,13970089.0,10.1016/S0021-9258(18)81322-9,,['eng'],238,-,702-9,The Journal of biological chemistry,-,Feb 1963,"W S BECK, M LEVIN"
+408,63BER/HOL,14087284.0,,,['ger'],338,-,114-21,Biochemische Zeitschrift,-, 1963,"H U BERGMEYER, G HOLZ, H KLOTZSCH, G LANG"
+409,63CHE/RAW,,10.1016/0006-3002(63)91239-3,,-,-,-,-,-,-,-,-
+410,63DAY/WIL,,10.1016/0006-3002(63)90519-5,,-,-,-,-,-,-,-,-
+411,63DEV/GOU,,10.1016/0926-6550(63)90451-1,,-,-,-,-,-,-,-,-
+412,63DOB/DEM,,10.1016/0006-3002(63)90547-X,,-,-,-,-,-,-,-,-
+413,63DOM/ZEC,14095156.0,,,['ger'],339,-,145-53,Biochemische Zeitschrift,-,Oct 1963,"G F DOMAGK, R ZECH"
+414,63EDM/WRI,14109183.0,10.1016/S0021-9258(19)75304-6,,['eng'],238,-,3539-41,The Journal of biological chemistry,-,Nov 1963,"J M EDMUNDOWICZ, J C WRISTON"
+415,63EHR/MAR,14109209.0,10.1016/S0021-9258(19)75330-7,,['eng'],238,-,3711-6,The Journal of biological chemistry,-,Nov 1963,"E EHRENFELD, S J MARBLE, A MEISTER"
+416,63FLA,,10.1016/0076-6879(63)06157-7,,-,-,-,-,-,-,-,-
+417,63FRI/SCH,13963148.0,10.1016/S0021-9258(19)68001-4,,['eng'],238,-,2509-17,The Journal of biological chemistry,-,Jul 1963,"I B FRITZ, S K SCHULTZ, P A SRERE"
+418,63GRE,,10.1016/0076-6879(63)06194-2,,-,-,-,-,-,-,-,-
+419,63HAR/COL,14063286.0,10.1016/S0021-9258(18)67880-9,,['eng'],238,-,2648-53,The Journal of biological chemistry,-,Aug 1963,"R J HARVEY, E B COLLINS"
+420,63HIN/WOL,14075112.0,10.1021/bi00904a025,,['eng'],2,-,770-5,Biochemistry,-, 1963,"M C HINES, R G WOLFE"
+421,63HUE,13955484.0,10.1021/bi00901a027,,['eng'],2,-,151-9,Biochemistry,-, 1963,F M HUENNEKENS
+422,63JEN/CAP,14093907.0,10.1021/bi00906a024,,['eng'],2,-,1313-20,Biochemistry,-, 1963,"W P JENCKS, M CAPLOW, M GILCHRIST, R G KALLEN"
+423,63KUR/FUK,,10.1016/0006-3002(63)91027-8,,-,-,-,-,-,-,-,-
+424,63MAP/ISH,13932735.0,10.1042/bj0860173,,['eng'],86,1,173-91,The Biochemical journal,-,Jan 1963,"L W MAPSON, F A ISHERWOOD"
+425,63MAR/BAR,,10.1016/S0021-9258(18)81106-1,,-,-,-,-,-,-,-,-
+426,63MAT/HUE,14085400.0,10.1016/S0021-9258(18)48686-3,,['eng'],238,-,3436-42,The Journal of biological chemistry,-,Oct 1963,"C K MATHEWS, F M HUENNEKENS"
+427,63MEI/BUK,14087295.0,,,['eng'],338,-,217-29,Biochemische Zeitschrift,-, 1963,"A MEISTER, M W BUKENBERGER, M STRASSBURGER"
+428,63MON/WHI,13936004.0,10.1016/S0021-9258(18)81333-3,,['eng'],238,-,767-74,The Journal of biological chemistry,-,Feb 1963,"C MONDER, A WHITE"
+429,63OKA,,10.1093/oxfordjournals.jbchem.a127721,,-,-,-,-,-,-,-,-
+430,63QUA,13972708.0,10.1042/bj0870368,,['eng'],87,2,368-73,The Biochemical journal,-,May 1963,J R QUAYLE
+431,63SCO/DUN,14086726.0,10.1016/S0021-9258(18)51808-1,,['eng'],238,-,3928-33,The Journal of biological chemistry,-,Dec 1963,"E M SCOTT, I W DUNCAN, V EKSTRAND"
+432,63SLY/STA,14063285.0,10.1016/S0021-9258(18)67879-2,,['eng'],238,-,2639-47,The Journal of biological chemistry,-,Aug 1963,"W S SLY, E R STADTMAN"
+433,63VIL/LAR,,10.1016/0076-6879(63)06186-3,,-,-,-,-,-,-,-,-
+434,64ADA/NOR,14189888.0,10.1016/S0021-9258(18)91347-5,,['eng'],239,-,1525-35,The Journal of biological chemistry,-,May 1964,"E ADAMS, I L NORTON"
+435,64ASP/JAK,14154441.0,10.1016/S0021-9258(18)51644-6,,['eng'],239,-,710-3,The Journal of biological chemistry,-,Mar 1964,"A J ASPEN, W B JAKOBY"
+436,64AVI,14257584.0,10.1016/S0021-9258(18)91180-4,,['eng'],239,-,3613-8,The Journal of biological chemistry,-,Nov 1964,G AVIGAD
+437,64BAR/ROO,14245371.0,10.1016/S0021-9258(18)97713-6,,['eng'],239,-,3260-6,The Journal of biological chemistry,-,Oct 1964,"H A BARKER, V ROOZE, F SUZUKI, A A IODICE"
+438,64BOJ/GAU,14102876.0,10.1128/jb.87.1.75-80.1964,,['eng'],87,1,75-80,Journal of bacteriology,"Bojanowski, R. (University of Illinois, Urbana), Elizabeth Gaudy, R. C. Valentine, and R. S. Wolfe. Oxamic transcarbamylase of Streptococcus allantoicus. J. Bacteriol. 87:75-80. 1964.-An improved colorimetric assay for carbamyl oxamate, which allows the precise measurement of the activity of oxamic transcarbamylase, has been developed. Activity is maximum over the pH range from 8.3 to 8.7. A cation requirement is satisfied by 2.5 x 10(-3)m Mg(++) or Mn(++). The equilibrium constant for the phosphorolysis of carbamyl oxamic acid is 1.6, corresponding to a negative free energy change of -285 cal per mole.",Jan 1964,"R BOJANOWSKI, E GAUDY, R C VALENTINE, R S WOLFE"
+439,64HEN/CLE,14155095.0,10.1021/bi00891a007,,['eng'],3,-,338-45,Biochemistry,-,Mar 1964,"C P HENSON, W W CLELAND"
+440,64IMA/MOR,,10.1093/oxfordjournals.jbchem.a127970,,-,-,-,-,-,-,-,-
+441,64KEL/ALL,14235536.0,10.1016/S0021-9258(18)93888-3,,['eng'],239,-,2562-9,The Journal of biological chemistry,-,Aug 1964,"R W KELLERMEYER, S H ALLEN, R STJERNHOLM, H G WOOD"
+442,64LOW/PAS,14114860.0,10.1016/S0021-9258(18)51741-5,,['eng'],239,-,31-42,The Journal of biological chemistry,-,Jan 1964,"O H LOWRY, J V PASSONNEAU"
+443,64MAI/DEK,14193832.0,10.1016/S0021-9258(18)91340-2,,['eng'],239,-,1485-91,The Journal of biological chemistry,-,May 1964,"U MAITRA, E E DEKKER"
+444,64MCN/DAM,14247682.0,10.1016/S0021-9258(18)91169-5,,['eng'],239,-,4272-9,The Journal of biological chemistry,-,Dec 1964,"W S MCNUTT, S P DAMLE"
+445,64MEL/WOO,14245410.0,10.1016/S0021-9258(18)97752-5,,['eng'],239,-,3511-4,The Journal of biological chemistry,-,Oct 1964,"H P MELOCHE, W A WOOD"
+446,64MIL/AVI,,10.1002/ijch.196400064,,-,-,-,-,-,-,-,-
+447,64MOO/REI,14245401.0,10.1016/S0021-9258(18)97743-4,,['eng'],239,-,3445-52,The Journal of biological chemistry,-,Oct 1964,"E C MOORE, P REICHARD, L THELANDER"
+448,64NOR,,10.1016/0926-6569(64)90103-8,,-,-,-,-,-,-,-,-
+449,64PRE/WOO,14245350.0,10.1016/S0021-9258(18)97692-1,,['eng'],239,-,3119-26,The Journal of biological chemistry,-,Oct 1964,"J PREISS, E WOOD"
+450,64ROS/RAP,,10.1038/201185a0,,-,-,-,-,-,-,-,-
+451,64SAT/TSU,,10.1246/nikkashi1898.67.5_683,,-,-,-,-,-,-,-,-
+452,64TAK/SAW,,10.1016/0926-6569(64)90263-9,,-,-,-,-,-,-,-,-
+453,64WIL/HOG,14235524.0,10.1016/S0021-9258(18)93876-7,,['eng'],239,-,2469-81,The Journal of biological chemistry,-,Aug 1964,"D B WILSON, D S HOGNESS"
+454,64ZAN/BAC,14127579.0,10.1128/JB.87.3.614-618.1964,,['eng'],87,3,614-8,Journal of bacteriology,"Zancan, Glaci T. (Universidade do Paraná, Curitiba, Paraná, Brazil), and Metry Bacila. Fructose-6-phosphate reductase from Salmonella gallinarum. J. Bacteriol. 87:614-618. 1964.-A fructose-6-phosphate reductase present in cell-free extracts of Salmonella gallinarum was purified approximately 42 times. The optimal pH for this enzyme is 8.0. The enzyme is specific for fructose-6-phosphate and reduced nicotinamide adenine dinucleotide (NADH). The dissociation constants are 1.78 x 10(-4)m for fructose-6-phosphate and 8.3 x 10(-5)m for NADH. The Q(10), reaction order, and equilibrium constant were determined. The enzyme is sensitive to p-chloromercuribenzoic acid, but not to o-iodosobenzoic acid nor to N-ethylmaleimide.",Mar 1964,"G T ZANCAN, M BACILA"
+455,65AND/ALL,14304839.0,10.1016/S0021-9258(18)97332-1,,['eng'],240,-,2367-72,The Journal of biological chemistry,-,Jun 1965,"R L ANDERSON, D P ALLISON"
+456,65ANN/KOS,,10.1139/o65-208,,-,-,-,-,-,-,-,-
+457,65BAH/CAT,14321375.0,10.1016/S0021-9258(18)97227-3,,['eng'],240,-,3372-8,The Journal of biological chemistry,-,Aug 1965,"J T BAHR, R E CATHOU, G G HAMMES"
+458,65BES/HER,14253449.0,10.1016/S0021-9258(18)97668-4,,['eng'],240,-,439-45,The Journal of biological chemistry,-,Jan 1965,"M J BESSMAN, S T HERRIOTT, M J ORR"
+459,65BOY/BAR,,10.1021/bi00885a020,,-,-,-,-,-,-,-,-
+460,65BUL/HAN,14321365.0,10.1016/S0021-9258(18)97216-9,,['eng'],240,-,3283-94,The Journal of biological chemistry,-,Aug 1965,"B BULOS, P HANDLER"
+461,65CAN/FOC,14321360.0,10.1016/S0021-9258(18)97211-X,,['eng'],240,-,3249-57,The Journal of biological chemistry,-,Aug 1965,"J J CANNATA, A FOCESI, R MAZUMDER, R C WARNER, S OCHOA"
+462,65CAR/KIR,,10.1016/S0926-6593(65)80047-9,,-,-,-,-,-,-,-,-
+463,65CHI/FEI,,10.1016/0006-291X(65)90155-5,,-,-,-,-,-,-,-,-
+464,65DAW/DIC,14346088.0,10.1042/bj0940353,,['eng'],94,2,353-67,The Biochemical journal,"1. The interconversion of hydroxypyruvate and l-glycerate in the presence of NAD and rat-liver l-lactate dehydrogenase has been demonstrated. Michaelis constants for these substrates together with an equilibrium constant have been determined and compared with those for pyruvate and l-lactate. 2. The presence of d-glycerate dehydrogenase in rat liver has been confirmed and the enzyme has been purified 16-20-fold from the supernatant fraction of a homogenate, when it is free of l-lactate dehydrogenase, with a 23-29% recovery. The enzyme catalyses the interconversion of hydroxypyruvate and d-glycerate in the presence of either NAD or NADP with almost equal efficiency. d-Glycerate dehydrogenase also catalyses the reduction of glyoxylate, but is distinct from l-lactate dehydrogenase in that it fails to act on pyruvate, d-lactate or l-lactate. The enzyme is strongly dependent on free thiol groups, as shown by inhibition with p-chloromercuribenzoate, and in the presence of sodium chloride the reduction of hydroxypyruvate is activated. Michaelis constants for these substrates of d-glycerate dehydrogenase and an equilibrium constant for the NAD-catalysed reaction have been calculated. 3. An explanation for the lowered V(max.) with d-glycerate as compared with dl-glycerate for the rabbit-kidney d-alpha-hydroxy acid dehydrogenase has been proposed.",Feb 1965,"P D DAWKINS, F DICKENS"
+465,65EIC/CYN,14285233.0,10.1021/bi00877a024,,['eng'],4,-,159-65,Biochemistry,-,Jan 1965,"M M EICHHORN, M A CYNKIN"
+466,65GAU/WOL,5854583.0,10.1128/jb.90.6.1531-1536.1965,,['eng'],90,6,1531-6,Journal of bacteriology,"Gaudy, Elizabeth T. (University of Illinois, Urbana), and R. S. Wolfe. Ureidoglycolate synthetase of Streptococcus allantoicus. II. Properties of the enzyme and reaction equilibrium. J. Bacteriol. 90:1531-1536. 1965.-The properties of ureidoglycolate synthetase from Streptococcus allantoicus grown on allantoin were studied, by use of the purified enzyme preparation and crystalline sodium ureidoglycolate. Ureidoglycolate synthetase activity was maximal over the pH range of 8.4 to 8.8. No cofactors were required for the reaction. Enzyme activity was inhibited by p-chloromercuribenzoate at relatively high concentrations, by Hg(++) or Zn(++) ions, and to a lesser extent by several other metal cations. The maximal velocity for the purified ureidoglycolate synthetase, determined graphically from a Lineweaver-Burk plot, was 220 mumoles of glyoxylate formed per min per mg of protein. The substrate concentration required for half-maximal velocity was 3.3 x 10(-2)m. The equilibrium constant for the synthesis of ureidoglycolate was determined in a series of reaction mixtures covering a wide range of initial concentrations of reactants. The position of the equilibrium was not affected by a change in pH or by the presence of enzyme. The equilibrium constant for the reaction in the direction of synthesis was 7.6, corresponding to a negative free energy change of 1,230 cal per mole.",Dec 1965,"E T Gaudy, R S Wolfe"
+467,65GHO/ROS,14285487.0,10.1016/S0021-9258(18)97467-3,,['eng'],240,-,1525-30,The Journal of biological chemistry,-,Apr 1965,"S GHOSH, S ROSEMAN"
+468,65GHO/ROS2,14285488.0,10.1016/S0021-9258(18)97468-5,,['eng'],240,-,1531-6,The Journal of biological chemistry,-,Apr 1965,"S GHOSH, S ROSEMAN"
+469,65ICH/HIR,,10.1271/nogeikagaku1924.39.291,,-,-,-,-,-,-,-,-
+470,65KAT/BUC,14275142.0,10.1016/S0021-9258(17)45250-1,,['eng'],240,-,825-35,The Journal of biological chemistry,-,Feb 1965,"H M KATZEN, J M BUCHANAN"
+471,65KAZ/GRO,14256957.0,10.1016/S0021-9258(18)97615-5,,['eng'],240,-,64-7,The Journal of biological chemistry,-,Jan 1965,"Y KAZIRO, A GROSSMAN, S OCHOA"
+472,65LEE/DOB,16562063.0,10.1128/jb.90.3.653-660.1965,,['eng'],90,3,653-60,Journal of bacteriology,"Lee, Chin K. (North Carolina State of the University of North Carolina, Raleigh), and Walter J. Dobrogosz. Oxidative metabolism in Pediococcus pentosaceus. III. Glucose dehydrogenase system. J. Bacteriol. 90:653-660. 1965.-A method was developed for the purification of glucose dehydrogenase from Pediococcus pentosaceus Az-25-5. The procedures included treatments with protamine sulfate, ammonium sulfate, and heat in addition to acid precipitation, calcium phosphate adsorption and elution, and diethylaminoethyl-Sephadex column chromatography. The final preparation thus obtained was purified 255-fold and exhibited both similarities and dissimilarities to the same enzyme isolated from other sources. The enzyme is absolutely specific for nicotinamide adenine dinucleotide phosphate (NADP) as a cofactor, and oxidizes only glucose or its analogue 2-deoxyglucose via the following reversible reaction: beta-d-glucose + NADP right harpoon over left harpoon d-glucono-delta-lactone + NADPH(2) + H(+). K(m) values were 2.3 x 10(-2) for glucose and 2 x 10(-4) for NADP. Monovalent cations were required for stability of the enzyme and stimulated activity. The pH optimum was 7.0, and the equilibrium constant was determined to be 13.4 x 10(-7) at pH 6.4. Among the Lactobacillaceae, glucose dehydrogenase activity was found to be essentially limited to members of the genus Pediococcus. Studies on the enzymatic composition of P. pentosaceus viewed in conjunction with other available data led to the conclusion that this enzyme is not involved to any significant extent in the energy metabolism of this organism.",Sep 1965,"C K Lee, W J Dobrogosz"
+473,65MAR/JEN,4953710.0,10.1016/S0021-9258(18)97177-2,,['eng'],240,9,3538-46,The Journal of biological chemistry,-,Sep 1965,"M Martinez-Carrion, W T Jenkins"
+474,65MAY/GIN,14299608.0,10.1016/S0021-9258(18)97402-8,,['eng'],240,-,1900-4,The Journal of biological chemistry,-,May 1965,"R M MAYER, V GINSBURG"
+475,65MOR/JAM,16749122.0,10.1042/bj0970037,,['eng'],97,1,37-52,The Biochemical journal,"1. The forward and reverse reactions catalysed by ATP-creatine phosphotransferase have been studied kinetically at pH8.0 in the presence and absence of products, under conditions in which the free Mg(2+) concentration was maintained constant at 1mm. Thus at fixed pH the reaction may be considered as being bireactant and expressed as:MgATP(2-)+creatine(0)right harpoon over left harpoonMgADP(-)+phosphocreatine(2-)2. The initial-velocity pattern in the absence of products and the product-inhibition pattern have been determined. These are consistent with a random mechanism in which all steps are in rapid equilibrium except that concerned with the interconversion of the central ternary complexes, and in which two dead-end complexes (enzyme-MgADP-creatine and enzyme-MgATP-phosphocreatine) are formed. The results are in accord with previous suggestions that the enzyme possesses distinct sites for the combination of the nucleotide and guanidino substrates. 3. Values have been determined for the Michaelis and dissociation constants involved in the combination of each substrate with various enzyme forms. Although these values cannot be regarded as absolute, they appear to indicate that the presence of one substrate on the enzyme enhances the combination of the second substrate. In addition, it would seem that in the formation of the enzyme-MgADP-creatine complex the concentration of one reactant does not affect the combination of the other. This contrasts with the formation of the enzyme-MgATP-phosphocreatine complex, where each reactant hinders the combination of the other.",Oct 1965,"J F Morrison, E James"
+476,65ONO/HIR,,10.1093/oxfordjournals.jbchem.a128147,,-,-,-,-,-,-,-,-
+477,65PIN,,10.1051/jcp/1965620591,,-,-,-,-,-,-,-,-
+478,65SEK/SUN,,,,-,-,-,-,-,-,-,-
+479,65SHA/CLE,14299613.0,10.1016/S0021-9258(18)97409-0,,['eng'],240,-,1946-56,The Journal of biological chemistry,-,May 1965,"D H SHAH, W W CLELAND, J W PORTER"
+480,65STI/DIA,,,,-,-,-,-,-,-,-,-
+481,65STR,14284729.0,10.1016/S0021-9258(18)97564-2,,['eng'],240,-,1225-30,The Journal of biological chemistry,-,Mar 1965,H J STRECKER
+482,65TAK/HIR,,10.1093/oxfordjournals.jbchem.a128195,,-,-,-,-,-,-,-,-
+483,65TAK/YOS,,10.1093/oxfordjournals.jbchem.a128194,,-,-,-,-,-,-,-,-
+484,65TAT/DAT,14348207.0,10.1042/bj0940470,,['eng'],94,2,470-7,The Biochemical journal,"1. A method of preparation and purification of citrate oxaloacetate-lyase (EC 4.1.3.6) from Aerobacter aerogenes is described. 2. The equilibrium of this reaction has been determined at pH 8.4 and 25 degrees . It has been shown that K, i.e. [citrate(3-)]/[oxaloacetate(keto) (2-)][acetate (-)], is 3.08+/-0.72, but that K(app.), i.e. [total citrate]/[total oxaloacetate][total acetate], is markedly affected by the initial concentrations of the reactants and magnesium. 3. The free-energy change during the cleavage of citrate has been calculated and compared with data from other sources. 4. The free energy of hydrolysis of acetyl-CoA has been evaluated from the present data. 5. A detailed knowledge of the interactions of the reactants with metal ions has been shown to be important in the calculation of the equilibrium constant and related thermodynamic functions.",Feb 1965,"S S TATE, S P DATTA"
+485,65TSU/SAT,,10.1271/bbb1961.29.1129,,-,-,-,-,-,-,-,-
+486,65UYE/RAB,14285511.0,10.1016/S0021-9258(18)97492-2,,['eng'],240,-,1701-10,The Journal of biological chemistry,-,Apr 1965,"K UYEDA, J C RABINOWITZ"
+487,65WAL/SAL,4378782.0,10.1021/bi00882a015,,['eng'],4,6,1076-85,Biochemistry,-,Jun 1965,"D A Walsh, H J Sallach"
+488,65YOS,14284712.0,10.1016/S0021-9258(18)97547-2,,['eng'],240,-,1118-24,The Journal of biological chemistry,-,Mar 1965,A YOSHIDA
+489,65YOS/FRE,,10.1016/0926-6593(65)90009-3,,-,-,-,-,-,-,-,-
+490,66ALB/BAS,4287931.0,10.1016/S0021-9258(18)96559-2,,['eng'],241,12,2968-75,The Journal of biological chemistry,-,Jun 1966,"G J Albrecht, S T Bass, L L Seifert, R G Hansen"
+491,66ALL,4289051.0,10.1016/S0021-9258(18)96427-6,,['eng'],241,22,5266-75,The Journal of biological chemistry,-,Nov 1966,S H Allen
+492,66AVI/ENG,4379259.0,10.1016/S0021-9258(18)96926-7,,['eng'],241,2,373-8,The Journal of biological chemistry,-,Jan 1966,"G Avigad, S Englard, S Pifko"
+493,66BER/MOE,5982377.0,,,['ger'],344,2,167-89,Biochemische Zeitschrift,-,Mar 1966,"H U Bergmeyer, H Moellering"
+494,66CAR/HUL,16742459.0,10.1042/bj1010781,,['eng'],101,3,781-91,The Biochemical journal,"1. Two enzymes that catalyse the reduction of glyoxylate to glycollate have been separated and purified from a species of Pseudomonas. Their molecular weights were estimated as 180000. 2. Reduced nicotinamide nucleotides act as the hydrogen donators for the enzymes. The NADH-linked enzyme is entirely specific for its coenzyme but the NADPH-linked reductase shows some affinity towards NADH. 3. Both enzymes convert hydroxypyruvate into glycerate. 4. The glyoxylate reductases show maximal activity at pH6.0-6.8, are inhibited by keto acids and are strongly dependent on free thiol groups for activity. 5. The Michaelis constants for glyoxylate and hydroxypyruvate were found to be of a high order. 6. The reversibility of the reaction has been demonstrated for both glyoxylate reductases and the equilibrium constants were determined. 7. The reduction of glyoxylate and hydroxypyruvate is not stimulated by anions.",Dec 1966,"L N Cartwright, R P Hullin"
+495,66CHA/WIL,5924646.0,10.1016/S0021-9258(18)99776-0,,['eng'],241,18,4251-60,The Journal of biological chemistry,-,Sep 1966,"S H Chang, D R Wilken"
+496,66DED,,10.1016/0076-6879(66)08091-1,,-,-,-,-,-,-,-,-
+497,66DOM/ZEC,,10.1016/0076-6879(66)09115-8,,-,-,-,-,-,-,-,-
+498,66GIB/MOR,16749179.0,10.1042/bj0990021p,,['eng'],99,2,21P-40P,The Biochemical journal,-,May 1966,-
+499,66GOL/MAR,5901055.0,10.1016/S0021-9258(18)96955-3,,['eng'],241,1,45-50,The Journal of biological chemistry,-,Jan 1966,"S H Goldemberg, L R Maréchal, B C De Souza"
+500,66HAN/ALB,,10.1016/0076-6879(66)08042-X,,-,-,-,-,-,-,-,-
+501,66HAN/VER,,10.1016/0076-6879(66)08048-0,,-,-,-,-,-,-,-,-
+502,66HOR/HEN,4287985.0,10.1016/S0021-9258(18)96478-1,,['eng'],241,14,3404-8,The Journal of biological chemistry,-,Jul 1966,"M Hori, J F Henderson"
+503,66JEN/DAR,5912360.0,10.1016/S0021-9258(18)96541-5,,['eng'],241,12,2845-54,The Journal of biological chemistry,-,Jun 1966,"W T Jenkins, L D'Ari"
+504,66KIM/SUZ,5933869.0,10.1016/S0021-9258(18)96808-0,,['eng'],241,5,1099-113,The Journal of biological chemistry,-,Mar 1966,"K Kimata, S Suzuki"
+505,66MAR/COH,4958913.0,10.1016/S0021-9258(18)99770-X,,['eng'],241,18,4197-208,The Journal of biological chemistry,-,Sep 1966,"M Marshall, P P Cohen"
+506,66MAR/WAD,5924638.0,10.1016/S0021-9258(18)99761-9,,['eng'],241,18,4136-45,The Journal of biological chemistry,-,Sep 1966,"F S Markland, C L Wadkins"
+507,66MAT,5924649.0,10.1016/S0021-9258(18)99779-6,,['eng'],241,18,4275-82,The Journal of biological chemistry,-,Sep 1966,S Matsuhashi
+508,66MAT/STR,,10.1016/0076-6879(66)08061-3,,-,-,-,-,-,-,-,-
+509,66MUD/KLE,5961285.0,10.1021/bi00869a030,,['eng'],5,5,1653-60,Biochemistry,-,May 1966,"S H Mudd, W A Klee, P D Ross"
+510,66MUR/SUG,5941994.0,10.1016/0003-9861(66)90153-6,,['eng'],113,1,34-44,Archives of biochemistry and biophysics,-,Jan 1966,"T Murata, T Sugiyama, T Minamikawa, T Akazawa"
+511,66NAT,,10.1271/bbb1961.30.887,,-,-,-,-,-,-,-,-
+512,66REI,,10.1016/0076-6879(66)09112-2,,-,-,-,-,-,-,-,-
+513,66SCH,,10.1016/0926-6593(66)90039-7,,-,-,-,-,-,-,-,-
+514,66SCH/HOR,4381350.0,10.1016/0003-9861(66)90020-8,,['eng'],116,1,117-28,Archives of biochemistry and biophysics,-,Sep 1966,"B M Scher, B L Horecker"
+515,66SHU,,10.1016/0076-6879(66)09104-3,,-,-,-,-,-,-,-,-
+516,66STA/DEN,,10.1016/0926-6593(66)90144-5,,-,-,-,-,-,-,-,-
+517,66THO/NAN,5971743.0,10.1016/0003-9861(66)90126-3,,['eng'],117,1,65-74,Archives of biochemistry and biophysics,-,Oct 1966,"J F Thomson, S L Nance, K J Bush, P A Szczepanik"
+518,66TOO/WAK,,10.1016/0005-2760(66)90001-4,,-,-,-,-,-,-,-,-
+519,66UHR/MAR,5954807.0,10.1016/S0021-9258(18)96447-1,,['eng'],241,22,5428-35,The Journal of biological chemistry,-,Nov 1966,"M L Uhr, F Marcus, J F Morrison"
+520,66VER/ROD,5946626.0,10.1016/S0021-9258(18)96658-5,,['eng'],241,9,2007-13,The Journal of biological chemistry,-,May 1966,"H Verachtert, P Rodriguez, S T Bass, R G Hansen"
+521,66WIL/WAK,5330116.0,10.1016/S0021-9258(18)96625-1,,['eng'],241,10,2326-32,The Journal of biological chemistry,-,May 1966,"I P Williamson, S J Wakil"
+522,66WOO/DAV,4288897.0,10.1016/S0021-9258(18)96399-4,,['eng'],241,23,5692-704,The Journal of biological chemistry,-,Dec 1966,"H G Wood, J J Davis, H Lochmüller"
+523,67BAR,,10.1007/BF00406311,,-,-,-,-,-,-,-,-
+524,67DAN/YOS,,10.1271/bbb1961.31.284,,-,-,-,-,-,-,-,-
+525,67ENG/DAL,4384597.0,10.1042/bj1050691,,['eng'],105,2,691-5,The Biochemical journal,"1. Equilibrium constants for the oxidation of glutamate by NAD(+) and NADP(+), catalysed by glutamate dehydrogenase, have been measured in phosphate buffers of different ionic strengths and at several temperatures. 2. The equilibrium constants for both systems vary markedly with ionic strength. Thermodynamic values for the two systems obtained by extrapolation to zero ionic strength differ significantly from one another. The standard free-energy change for NADP(+) reduction has been calculated from that for NAD(+) reduction. 3. The heat of reaction has been estimated and is the same with both coenzymes. 4. The thermodynamic data are discussed in relation to earlier data.",Nov 1967,"P C Engel, K Dalziel"
+526,67ENG/DEN,5583983.0,10.1042/bj1050032c,,['eng'],105,2,32C-33C,The Biochemical journal,-,Nov 1967,"P J England, R M Denton, P J Randle"
+527,67EPP/DAW,6016604.0,10.1016/S0021-9258(19)81449-7,,['eng'],242,2,204-9,The Journal of biological chemistry,-,Jan 1967,"H M Eppenberger, D M Dawson, N O Kaplan"
+528,67GRO,6016328.0,10.1016/S0021-9258(18)96331-3,,['eng'],242,1,155-9,The Journal of biological chemistry,-,Jan 1967,D P Groth
+529,67HER/JEN,,10.1016/S0021-9258(18)95886-2,,-,-,-,-,-,-,-,-
+530,67HIR/GRE,6022873.0,10.1016/S0021-9258(18)96047-3,,['eng'],242,9,2283-7,The Journal of biological chemistry,-,May 1967,"H Hirsch, D M Greenberg"
+531,67KEP/TOV,5633396.0,10.1016/S0021-9258(18)99355-5,,['eng'],242,24,5686-92,The Journal of biological chemistry,-,Dec 1967,"C R Kepler, S B Tove"
+532,67LOM/GRE,6033708.0,10.1016/0003-9861(67)90352-9,,['eng'],118,2,297-304,Archives of biochemistry and biophysics,-,Feb 1967,"L Lombrozo, D M Greenberg"
+533,67MOR/WHI,6079774.0,10.1111/j.1432-1033.1967.tb19509.x,,['eng'],3,2,145-52,European journal of biochemistry,-,Dec 1967,"J F Morrison, A White"
+534,67PLO/CLE,6061708.0,10.1016/S0021-9258(18)95802-3,,['eng'],242,18,4239-47,The Journal of biological chemistry,-,Sep 1967,"D M Plowman, W W Cleland"
+535,67POE/GUT,4294746.0,10.1016/0003-9861(67)90140-3,,['eng'],122,1,204-11,Archives of biochemistry and biophysics,-,Oct 1967,"M Poe, H Gutfreund, R W Estabrook"
+536,67ROS/ADA,12325368.0,10.1016/S0021-9258(18)99389-0,,['eng'],242,23,5524-34,The Journal of biological chemistry,-,Dec 1967,"R G Rosso, E Adams"
+537,67SAK/YOR,,10.1271/bbb1961.31.525,,-,-,-,-,-,-,-,-
+538,67SAK/YOR2,,10.1271/bbb1961.31.533,,-,-,-,-,-,-,-,-
+539,67SIL/VOE,4381552.0,10.1016/S0021-9258(18)96185-5,,['eng'],242,6,1338-46,The Journal of biological chemistry,-,Mar 1967,"R Silverstein, J Voet, D Reed, R H Abeles"
+540,67SOD/OSU,,10.1271/bbb1961.31.1097,,-,-,-,-,-,-,-,-
+541,67TAK,,10.1271/bbb1961.31.309,,-,-,-,-,-,-,-,-
+542,67TAK/HIZ,,10.1016/0005-2744(67)90241-0,,-,-,-,-,-,-,-,-
+543,67TAK2,,10.1271/bbb1961.31.435,,-,-,-,-,-,-,-,-
+544,67TRI/VOG,,10.1016/0005-2744(67)90197-0,,-,-,-,-,-,-,-,-
+545,67UYE/RAB,4383631.0,10.1016/S0021-9258(18)99549-9,,['eng'],242,19,4378-85,The Journal of biological chemistry,-,Oct 1967,"K Uyeda, J C Rabinowitz"
+546,67WIL/HIR,,10.1016/0005-2744(67)90139-8,,-,-,-,-,-,-,-,-
+547,67WIL/LUN,4291787.0,10.1042/bj1030514,,['eng'],103,2,514-27,The Biochemical journal,"1. The concentrations of the oxidized and reduced substrates of the lactate-, beta-hydroxybutyrate- and glutamate-dehydrogenase systems were measured in rat livers freeze-clamped as soon as possible after death. The substrates of these dehydrogenases are likely to be in equilibrium with free NAD(+) and NADH, and the ratio of the free dinucleotides can be calculated from the measured concentrations of the substrates and the equilibrium constants (Holzer, Schultz & Lynen, 1956; Bücher & Klingenberg, 1958). The lactate-dehydrogenase system reflects the [NAD(+)]/[NADH] ratio in the cytoplasm, the beta-hydroxybutyrate dehydrogenase that in the mitochondrial cristae and the glutamate dehydrogenase that in the mitochondrial matrix. 2. The equilibrium constants of lactate dehydrogenase (EC 1.1.1.27), beta-hydroxybutyrate dehydrogenase (EC 1.1.1.30) and malate dehydrogenase (EC 1.1.1.37) were redetermined for near-physiological conditions (38 degrees ; I0.25). 3. The mean [NAD(+)]/[NADH] ratio of rat-liver cytoplasm was calculated as 725 (pH7.0) in well-fed rats, 528 in starved rats and 208 in alloxan-diabetic rats. 4. The [NAD(+)]/[NADH] ratio for the mitochondrial matrix and cristae gave virtually identical values in the same metabolic state. This indicates that beta-hydroxybutyrate dehydrogenase and glutamate dehydrogenase share a common pool of dinucleotide. 5. The mean [NAD(+)]/[NADH] ratio within the liver mitochondria of well-fed rats was about 8. It fell to about 5 in starvation and rose to about 10 in alloxan-diabetes. 6. The [NAD(+)]/[NADH] ratios of cytoplasm and mitochondria are thus greatly different and do not necessarily move in parallel when the metabolic state of the liver changes. 7. The ratios found for the free dinucleotides differ greatly from those recorded for the total dinucleotides because much more NADH than NAD(+) is protein-bound. 8. The bearing of these findings on various problems, including the following, is discussed: the number of NAD(+)-NADH pools in liver cells; the applicability of the method to tissues other than liver; the transhydrogenase activity of glutamate dehydrogenase; the physiological significance of the difference of the redox states of mitochondria and cytoplasm; aspects of the regulation of the redox state of cell compartments; the steady-state concentration of mitochondrial oxaloacetate; the relations between the redox state of cell compartments and ketosis.",May 1967,"D H Williamson, P Lund, H A Krebs"
+548,67WOL,6061417.0,10.1016/S0021-9258(18)99514-1,,['eng'],242,20,4711-4,The Journal of biological chemistry,-,Oct 1967,R Wolfenden
+549,67WU/WIT,,10.1021/ja00985a003,,-,-,-,-,-,-,-,-
+550,68AUR/KLE,4302217.0,10.1111/j.1432-1033.1968.tb00437.x,,['ger'],6,2,196-201,European journal of biochemistry,-,Nov 1968,"H Aurich, H P Kleber, H Sorger, H Tauchert"
+551,68AVI/ALR,4384672.0,10.1016/S0021-9258(18)93531-3,,['eng'],243,8,1936-41,The Journal of biological chemistry,-,Apr 1968,"G Avigad, Y Alroy, S Englard"
+552,68AYL/SNE,5650370.0,10.1021/bi00845a002,,['eng'],7,5,1616-25,Biochemistry,-,May 1968,"J E Ayling, E E Snell"
+553,68AYL/SNE2,5650371.0,10.1021/bi00845a003,,['eng'],7,5,1626-36,Biochemistry,-,May 1968,"J E Ayling, E E Snell"
+554,68BAD/MIL,5681454.0,10.1021/bi00850a014,,['eng'],7,10,3403-8,Biochemistry,-,Oct 1968,"J L Bada, S L Miller"
+555,68BEE/DEL,,10.1111/j.1432-1033.1968.tb00453.x,,-,-,-,-,-,-,-,-
+556,68BOM/PRA,,10.1016/0005-2728(68)90105-9,,-,-,-,-,-,-,-,-
+557,68BRO,,,,-,-,-,-,-,-,-,-
+558,68BUR/WAL,,10.1016/0005-2744(68)90028-4,,-,-,-,-,-,-,-,-
+559,68DYS/NOL,5647261.0,10.1016/S0021-9258(18)93559-3,,['eng'],243,7,1401-14,The Journal of biological chemistry,-,Apr 1968,"J E Dyson, E A Noltmann"
+560,68ERI,,10.1111/j.1365-2621.1968.tb03667.x,,-,-,-,-,-,-,-,-
+561,68HAT/SLA,4305612.0,10.1042/bj1060141,,['eng'],106,1,141-6,The Biochemical journal,"1. An enzyme was isolated from leaves of tropical grasses that catalyses the reversible conversion of pyruvate, ATP and orthophosphate into phosphopyruvate, AMP and pyrophosphate. A requirement for Mg(2+) could not be replaced by Mn(2+) or Ca(2+). 2. By replacing orthophosphate with [(32)P]orthophosphate or with arsenate, evidence was provided that the orthophosphate consumed appears in pyrophosphate. 3. Without Mg(2+) or 2-mercaptoethanol the enzyme was rapidly and irreversibly inactivated. EDTA only partially replaced the requirement for the thiol compound. The enzyme was considerably more unstable at 0 degrees or when frozen than at 22 degrees . Even with the best conditions devised the enzyme lost about 25% of its activity every 3hr. 4. The activities of the enzyme in leaves of the tropical grasses sugar cane (Saccharum hybrid var. Pindar), maize (Zea mays) and sorghum (Sorghum vulgare) were comparable with their maximum photosynthesis rates. The enzyme was not detectable in leaf extracts from several other plants. 5. Its role in photosynthesis is discussed.",Jan 1968,"M D Hatch, C R Slack"
+562,68HAV/HAN,5655435.0,10.1021/bi00845a039,,['eng'],7,5,1904-14,Biochemistry,-,May 1968,"E A Havir, K R Hanson"
+563,68JEA/DEM,,10.1139/m68-068,,-,-,-,-,-,-,-,-
+564,68KOH,4300866.0,10.1016/S0021-9258(18)93210-2,,['eng'],243,17,4426-33,The Journal of biological chemistry,-,Sep 1968,L E Kohn
+565,68KOH/JAK,4297260.0,10.1016/S0021-9258(18)93399-5,,['eng'],243,10,2472-8,The Journal of biological chemistry,-,May 1968,"L D Kohn, W B Jakoby"
+566,68KOH/JAK2,4385076.0,10.1016/S0021-9258(18)93401-0,,['eng'],243,10,2486-93,The Journal of biological chemistry,-,May 1968,"L D Kohn, W B Jakoby"
+567,68LON/DAL,4387224.0,10.1042/bj1100217,,['eng'],110,2,217-22,The Biochemical journal,"1. The equilibrium constant for oxidative decarboxylation of isocitrate by NADP(+), catalysed by isocitrate dehydrogenase, was measured in solutions of various ionic strengths and at several temperatures. 2. Thermodynamic values for the reaction were obtained by extrapolation to zero ionic strength, and the heat of reaction was estimated. 3. The effect of Mg(2+) ion concentration on the equilibrium was studied.",Nov 1968,"J C Londesborough, K Dalziel"
+568,68MAY/AND,5726889.0,10.1016/S0021-9258(18)93144-3,,['eng'],243,24,6330-3,The Journal of biological chemistry,-,Dec 1968,"J W Mayo, R L Anderson"
+569,68MIZ/WEE,5658542.0,10.1016/S0021-9258(19)34190-0,,['eng'],243,13,3661-70,The Journal of biological chemistry,-,Jul 1968,"M Mizugaki, G Weeks, R E Toomey, S J Wakil"
+570,68NIX/BLA,5687716.0,10.1016/S0021-9258(18)93178-9,,['eng'],243,18,4722-31,The Journal of biological chemistry,-,Sep 1968,"P F Nixon, R L Blakley"
+571,68POT/GLO,5690817.0,10.1016/S0021-9258(18)92023-5,,['eng'],243,14,3864-70,The Journal of biological chemistry,-,Jul 1968,"L T Potter, V A Glover, J K Saelens"
+572,68REE/MEN,4302788.0,10.1016/S0021-9258(18)91972-1,,['eng'],243,20,5486-91,The Journal of biological chemistry,-,Oct 1968,"R E Reeves, R A Menzies, D S Hsu"
+573,68SAL/NOR,,10.1016/0005-2744(68)90116-2,,-,-,-,-,-,-,-,-
+574,68SU/RUS,5661709.0,10.1016/S0021-9258(18)92018-1,,['eng'],243,14,3826-33,The Journal of biological chemistry,-,Jul 1968,"S Su, P J Russell"
+575,68SUG/PIZ,4384871.0,10.1016/S0021-9258(18)93450-2,,['eng'],243,9,2081-9,The Journal of biological chemistry,-,May 1968,"E Sugimoto, L I Pizer"
+576,68TAN/KAN,5655499.0,10.1111/j.1432-1033.1968.tb00199.x,,['eng'],4,2,233-9,European journal of biochemistry,-,Apr 1968,"W Tanner, O Kandler"
+577,68VEE,,,,-,-,-,-,-,-,-,-
+578,69ALB,,10.1016/S0021-9258(18)93127-3,,-,-,-,-,-,-,-,-
+579,69BAR,,,,-,-,-,-,-,-,-,-
+580,69BEN,,,,-,-,-,-,-,-,-,-
+581,69BLA,5781279.0,10.1111/j.1432-1033.1969.tb00526.x,,['eng'],8,2,287-91,European journal of biochemistry,-,Mar 1969,J M Blair
+582,69BLA/FRA,5824560.0,10.1016/S0021-9258(18)94283-3,,['eng'],244,18,4864-70,The Journal of biological chemistry,-,Sep 1969,"F Blasi, F Fragomele, I Covelli"
+583,69BRE/AAS,,,,-,-,-,-,-,-,-,-
+584,69DAH/AND,,10.1016/0006-291X(69)90681-0,,-,-,-,-,-,-,-,-
+585,69DOL,4310090.0,10.1016/S0021-9258(18)63657-9,,['eng'],244,19,5273-85,The Journal of biological chemistry,-,Oct 1969,M I Dolin
+586,69FAN/FEI,16657106.0,10.1104/pp.44.4.599,,['eng'],44,4,599-604,Plant physiology,"Uridine diphosphate (UDP)-glucose 4-epimerase (EC 5.1.3.2) has been purified over 1000-fold from extracts of wheat germ by MnCl(2) treatment, (NH(4))(2)SO(4) fractionation, Sephadex column chromatography, and adsorption onto and elution from calcium phosphate gel. The enzyme has a pH optimum of 9.0. Km values are 0.1 mm for UDP-d-galactose and 0.2 mm for UDP-d-glucose. NAD is required for activity; K(a) = 0.04 mm. NADH is an inhibitor strictly competitive with NAD; K(i) = 2 mum. Wheat germ also contains UDP-l-arabinose 4-epimerase (EC 5.1.3.5) and thymidine diphosphate (TDP)-glucose 4-epimerase which are distinct from UDP-glucose 4-epimerase.",Apr 1969,"D F Fan, D S Feingold"
+587,69GAR/CLE,5793714.0,10.1021/bi00830a026,,['eng'],8,2,633-40,Biochemistry,-,Feb 1969,"E Garces, W W Cleland"
+588,69GEO/TRA,,,,-,-,-,-,-,-,-,-
+589,69GRE/RUD,4309154.0,10.1016/S0021-9258(18)93695-1,,['eng'],244,17,4798-800,The Journal of biological chemistry,-,Sep 1969,"P Greengard, S A Rudolph, J M Sturtevant"
+590,69KLO,,10.1016/0076-6879(69)13065-7,,-,-,-,-,-,-,-,-
+591,69LAN/DEK,4309127.0,10.1021/bi00835a041,,['eng'],8,7,2958-66,Biochemistry,-,Jul 1969,"R S Lane, E E Dekker"
+592,69PAS/LOW,5814030.0,10.1016/S0021-9258(18)91871-5,,['eng'],244,3,902-9,The Journal of biological chemistry,-,Feb 1969,"J V Passonneau, O H Lowry, D W Schulz, J G Brown"
+593,69PET/MCK,4306134.0,10.1016/0003-9861(69)90128-3,,['eng'],131,1,245-52,Archives of biochemistry and biophysics,-,Apr 1969,"J A Peterson, E J McKenna, D W Estabrook, M J Coon"
+594,69POP,,10.1016/S0076-6879(69)15014-4,,-,-,-,-,-,-,-,-
+595,69ROS/HAM,5814934.0,10.1021/bi00833a017,,['eng'],8,5,1884-9,Biochemistry,-,May 1969,"E J del Rosario, G G Hammes"
+596,69SHE/ALE,5773308.0,10.1016/S0021-9258(18)94451-0,,['eng'],244,2,457-64,The Journal of biological chemistry,-,Jan 1969,"K Sheth, J K Alexander"
+597,69SMI/MOR,5800442.0,10.1016/S0021-9258(17)36405-0,,['eng'],244,15,4224-34,The Journal of biological chemistry,-,Aug 1969,"E Smith, J F Morrison"
+598,69SWI,4306285.0,10.1016/S0021-9258(18)91705-9,,['eng'],244,11,2854-63,The Journal of biological chemistry,-,Jun 1969,R L Switzer
+599,69TSU/FUK,5782905.0,10.1016/S0021-9258(18)91886-7,,['eng'],244,3,1008-15,The Journal of biological chemistry,-,Feb 1969,"K K Tsuboi, K Fukunaga, J C Petricciani"
+600,69VEE/EGG,4391039.0,10.1042/bj1150609a,,['eng'],115,4,609-19,The Biochemical journal,"1. The concentrations of the oxidized and reduced substrates of the ;malic' enzyme (EC 1.1.1.40) and isocitrate dehydrogenase (EC 1.1.1.42) were measured in freeze-clamped rat livers. By assuming that the reactants of these dehydrogenase systems are at equilibrium in the cytoplasm the [free NADP(+)]/[free NADPH] ratio was calculated. The justification of the assumption is discussed. 2. The values of this ratio obtained under different nutritional conditions (well-fed, 48hr.-starved, fed with a low-carbohydrate diet, fed with a high-sucrose diet) were all of the same order of magnitude although characteristic changes occurred on varying the diet. The value of the ratio fell on starvation and on feeding with the low-carbohydrate diet and rose slightly on feeding with the high-sucrose diet. 3. The mean values of the ratio were calculated to be between 0.001 and 0.015, which is about 100000 times lower than the values of the cytoplasmic [free NAD(+)]/[free NADH] ratio. 4. The differences in the redox state of the two nicotinamide-adenine dinucleotide couples can be explained on a simple physicochemical basis. The differences are the result of equilibria that are determined by the equilibrium constants of a number of highly active readily reversible dehydrogenases and transaminases and the concentrations of the substrates and products of these enzymes. 5. The decisive feature is the fact that the NAD and NADP couples share substrates. This sharing provides a link between the redox states of the two couples. 6. The application of the method of calculation to data published by Kraupp, Adler-Kastner, Niessner & Plank (1967), Goldberg, Passonneau & Lowry (1966) and Kauffman, Brown, Passonneau & Lowry (1968) shows that the redox states of the NAD and NADP couples in cardiac-muscle cytoplasm and in mouse-brain cytoplasm are of the same order as those in rat liver. 7. The determination of the equilibrium constant at 38 degrees , pH7.0 and I 0.25 (required for the calculation of the [free NADP(+)]/[free NADPH] ratio), gave a value of 3.44x10(-2)m for the ;malic' enzyme (with CO(2) rather than HCO(3) (-) as the reactant) and a value of 1.98x10(-2)m(-1) for glutathione reductase.",Dec 1969,"R L Veech, L V Eggleston, H A Krebs"
+601,69VEE/RAI,5357024.0,10.1042/bj1150837,,['eng'],115,4,837-42,The Biochemical journal,"1. The equilibrium constant at 38 degrees and I 0.25 of the triose phosphate isomerase reaction was found to be 22.0 and that of the aldolase reaction, 0.99x10(-4)m. The [dihydroxyacetone phosphate]/[glyceraldehyde phosphate] ratio was found to be 9.3 in rat liver. The causes of the apparent deviation of the triose phosphate isomerase system from equilibrium in vivo have been investigated. 2. The equilibria of the triose phosphate isomerase and aldolase reactions were studied with relatively large concentrations of crystalline enzymes and small concentrations of substrates, approximating to those found in rat liver and muscle. There was significant binding of fructose diphosphate by aldolase under these conditions. There was no evidence that binding of glyceraldehyde phosphate by either enzyme affected the equilibria. 3. The deviation from equilibrium of the triose phosphate isomerase system in rat liver can be accounted for by the low activity of the enzyme, in relation to the flux, at low physiological concentrations of glyceraldehyde phosphate (about 3mum). It has been calculated that a flux of 1.8mumoles/min./g. wet weight of liver would be expected to cause the measured degree of disequilibrium found in vivo. 4. The conclusion that the triose phosphate isomerase is not at equilibrium is in accordance with the situation postulated by Rose, Kellermeyer, Stjernholm & Wood (1962) on the basis of isotope-distribution data. 5. The triose phosphate isomerase system is closer to equilibrium in resting muscle probably because of a very low flux and a high enzyme concentration. 6. The aldolase system deviated from equilibrium in rat liver by a factor of about 10 and by a much greater factor in resting muscle. 7. The measurement of total dihydroxyacetone phosphate and glyceraldehyde phosphate content indicates the concentrations of the free metabolites in the tissue. This may not hold for fructose diphosphate, a significant proportion of which may be bound to aldolase.",Dec 1969,"R L Veech, L Raijman, K Dalziel, H A Krebs"
+602,69VIL/DAL,4391041.0,10.1042/bj1150633,,['eng'],115,4,633-8,The Biochemical journal,"1. It was shown that dissolved CO(2) and not HCO(3) (-) or H(2)CO(3) is the primary substrate for reductive carboxylation with 6-phosphogluconate dehydrogenase from sheep liver. 2. The equilibrium constant of the reaction was measured in solutions of various ionic strengths and at several temperatures, and the free energy and heat of reaction were determined.",Dec 1969,"R H Villet, K Dalziel"
+603,69WAN/BAR,5769987.0,10.1016/S0021-9258(18)83432-9,,['eng'],244,10,2516-26,The Journal of biological chemistry,-,May 1969,"C C Wang, H A Barker"
+604,69WHI/LEJ,4989322.0,10.1042/bj1130589,,['eng'],113,4,589-601,The Biochemical journal,"1. Diaminopimelate epimerase from a soluble extract of Bacillus megaterium N.C.I.B. 7581 was purified about 25-fold by fractionation with ammonium sulphate and chromatography on calcium phosphate gel-cellulose. The product was impure but was unstable on further purification. 2. Quantitative assay methods for the enzyme were devised in which meso- or ll-diaminopimelic acid may be the substrate. 3. Between 25 degrees and 45 degrees at pH7.0 enzyme action leads to an equilibrium mixture containing 65% meso-isomer and 35% ll-isomer. 4. The initial rate of epimerization was 2-3 times as fast with ll-diaminopimelic acid as substrate as with the meso-isomer; a number of other amino acids were not racemized by the enzyme. The Michaelis constants at 37 degrees were 6.7mm (ll-isomer) and 100mm (meso-isomer); with both substrates enzyme activity was maximal at pH7-8. The relative rates of epimerization of ll-diaminopimelic acid at 25 degrees , 37 degrees and 45 degrees were 0.77:1.00:1.15. 5. A thiol compound (of which 2,3-dimercaptopropan-1-ol was the most effective) was needed as an activator of the purified enzyme. 6. Carbonylbinding reagents and several other compounds did not inhibit diaminopimelate epimerase. 7. Pyridoxal phosphate did not stimulate enzymic activity even in preparations that had been almost completely freed of derivatives of vitamin B(6) (as shown by microbiological assay).",Jul 1969,"P J White, B Lejeune, E Work"
+605,70ALB,5423264.0,10.1021/bi00814a011,,['eng'],9,12,2462-70,Biochemistry,-,Jun 1970,G J Albrecht
+606,70BAL/DEN,,10.1016/0076-6879(71)17212-6,,-,-,-,-,-,-,-,-
+607,70BEN/FRI,5442269.0,10.1016/S0021-9258(18)63142-4,,['eng'],245,9,2219-28,The Journal of biological chemistry,-,May 1970,"R L Benson, S Friedman"
+608,70BLA,4245368.0,10.1111/j.1432-1033.1970.tb00940.x,,['eng'],13,2,384-90,European journal of biochemistry,-,Apr 1970,J M Blair
+609,70BRO/KRE,4316090.0,10.1042/bj1170091,,['eng'],117,1,91-6,The Biochemical journal,"1. Changes in the concentrations of ammonia, glutamine, glutamate, 2-oxoglutarate, 3-hydroxybutyrate, acetoacetate, alanine, aspartate, malate, lactate, pyruvate, NAD(+), NADH and adenine nucleotides were measured in freeze-clamped rat liver during ischaemia. 2. Although the concentrations of most of the metabolites changed rapidly during ischaemia the ratios [glutamate]/[2-oxoglutarate][NH(4) (+)] and [3-hydroxybutyrate]/[acetoacetate] changed equally and the value of the expression [3-hydroxybutyrate][2-oxoglutarate][NH(4) (+)]/[acetoacetate][glutamate] remained approximately constant, indicating that the 3-hydroxybutyrate dehydrogenase and glutamate dehydrogenase systems were at near-equilibrium with the mitochondrial NAD(+) couple. 3. The value of the expression [alanine][oxoglutarate]/[pyruvate][glutamate] was about 0.7 in vivo and remained fairly constant during the ischaemic period of 5min, although the concentrations of alanine and oxoglutarate changed substantially. No explanation can be offered why the value of the ratio differed from that of the equilibrium constant of the alanine aminotransferase reaction, which is 1.48. 4. Injection of l-cycloserine 60min before the rats were killed increased the concentration of alanine in the liver fourfold and decreased the concentration of the other metabolites measured, except that of pyruvate. During ischaemia the concentration of alanine did not change but that of aspartate almost doubled. 5. After treatment with l-cycloserine the value in vivo of the expression [alanine][oxoglutarate]/[pyruvate][glutamate] rose from 0.7 to 2.4. During ischaemia the value returned to 0.8. 6. The effects of l-cycloserine are consistent with the assumption that it specifically inhibits alanine aminotransferase. 7. Most of the alanine formed during ischaemia is probably derived from pyruvate and from ammonia released by the deamination of adenine nucleotides and glutamine. The alanine is presumably formed by the combined action of glutamate dehydrogenase and alanine aminotransferase. 8. The rate of anaerobic glycolysis, calculated from the increase in the lactate concentration, was 1.3mumol/min per g fresh wt. 9. Although the concentrations of the adenine nucleotides changed rapidly during ischaemia, the ratio [ATP][AMP]/[ADP](2) remained constant at 0.54, indicating that adenylate kinase established near-equilibrium under these conditions.",Mar 1970,"J T Brosnan, H A Krebs, D H Williamson"
+610,70CHI/ZAP,5438361.0,10.1016/S0021-9258(19)77160-9,,['eng'],245,7,1778-89,The Journal of biological chemistry,-,Apr 1970,"T P Chirpich, V Zappia, R N Costilow, H A Barker"
+611,70DEN,,10.1016/0076-6879(71)17195-9,,-,-,-,-,-,-,-,-
+612,70FAN/FEI,5483919.0,10.1104/pp.46.4.592,,['eng'],46,4,592-5,Plant physiology,"Uridine diphosphate (UDP)-arabinose 4-epimerase (EC 5.1.3.5) has been purified at least 20-fold from wheat germ by MnCl(2) treatment, (NH(4))(2)SO(4) fractionation, dialysis, and Sephadex and diethylaminoethyl cellulose column chromatography. The enzyme has no action on UDP-d-glucose, UDP-d-glucuronic acid, or TDP-d-glucose. The pH optimum is 8.0. Km values are 1.5 mM for UDP-d-xylose and 0.5 mm for UDP-l-arabinose. The equilibrium constant, K, for the reaction UDP-l-arabinose left arrow over right arrow UDP-d-xylose is 1.25. The enzyme is neither activated by nicotinamide adenine dinucleotide nor inhibited by reduced nicotinamide adenine dinucleotide. It is completely inhibited by p-chloromercuri-phenylsulfonate; the inhibition is reversed by cysteine.",Oct 1970,"D F Fan, D S Feingold"
+613,70GEO/WIT,,10.1016/0005-2728(70)90126-X,,-,-,-,-,-,-,-,-
+614,70HER,5470822.0,10.1016/S0021-9258(18)62958-8,,['eng'],245,14,3526-35,The Journal of biological chemistry,-,Jul 1970,L B Hersh
+615,70HEY/ELB,5438047.0,10.1128/jb.101.3.777-780.1970,,['eng'],101,3,777-80,Journal of bacteriology,"An enzyme, d-mannose ketol isomerase, catalyzing the isomerization of d-mannose and d-fructose was purified approximately 60-fold from cells of Mycobacterium smegmatis grown on mannose as the sole carbon source. This enzyme was shown to catalyze the conversion of d-mannose and d-lyxose to ketoses. The ketose produced from mannose was identified as fructose by chemical and chromatographic methods. The reaction was shown to be reversible, the equilibrium ratio of fructose to mannose being approximately 65 to 35. The pH optimum was about 7.5, and the K(m) for mannose was estimated to be 7 x 10(-3)m. Mannose isomerase activity was greatest in cells grown on mannose, whereas cells grown on fructose had about 30% as much activity. Very low levels of activity were detected in cells grown on other substrates. There was an immediate increase in enzyme activity on transfer of cells from nutrient broth to a mannose mineral salts medium.",Mar 1970,"A Hey-Ferguson, A D Elbein"
+616,70JEN/TAY,,10.1016/0076-6879(71)17285-0,,-,-,-,-,-,-,-,-
+617,70KNO/HAN,5427280.0,10.1016/S0021-9258(18)63098-4,,['eng'],245,10,2499-504,The Journal of biological chemistry,-,May 1970,"J K Knop, R G Hansen"
+618,70KOH/WAR,4395378.0,10.1016/S0021-9258(18)62926-6,,['eng'],245,15,3831-9,The Journal of biological chemistry,-,Aug 1970,"L D Kohn, W A Warren"
+619,70KRI/BUC,5493986.0,10.1111/j.1432-1033.1970.tb01202.x,,['eng'],17,3,568-80,European journal of biochemistry,-,Dec 1970,"W K Krietsch, T Bücher"
+620,70MAN/HOL,4910853.0,10.1073/pnas.65.3.660,,['eng'],65,3,660-7,Proceedings of the National Academy of Sciences of the United States of America,"The reversibility of adenylylation of glutamine synthetase from E. coli by adenylyltransferase was demonstrated. Several positive effectors (Gln, 2-hydroxyethyl-S-cysteine, Trp and Met) stimulate the back reaction in the same manner as the forward reaction. The apparent Michaelis constant for PP(i) is 2.2 mM at pH 7.35. The pH optimum of the back reaction is 6.5-7 while the pH optimum of the forward reaction is 7.6. The apparent equilibrium constant in the presence of 10 mM Mg(2+) at pH 7.36 is 8.5 in favor of adenylylated glutamine synthetase and PP(i). The equilibrium constant is strongly dependent from pH and from Mg(2+) concentration. There is a difference of about 0.5 to 1 kcal/mole free energy between the adenylyl-O-tyrosine bond and the pyrophosphate bond of adenosine triphosphate (ATP). It follows from these considerations that the adenylyl-O-tyrosine bond is an ""energy-rich phosphate bond.""",Mar 1970,"M Mantel, H Holzer"
+621,70MAR/COH,,10.1016/0076-6879(71)17186-8,,-,-,-,-,-,-,-,-
+622,70NAK/FUJ,,10.1016/0005-2744(70)90054-9,,-,-,-,-,-,-,-,-
+623,70NAK/TSU,5498430.0,10.1016/S0021-9258(19)63814-7,,['eng'],245,17,4443-9,The Journal of biological chemistry,-,Sep 1970,"M Nakano, Y Tsutsumi, T S Danowski"
+624,70TSA/HOL,,10.1016/0003-9861(70)90347-4,,-,-,-,-,-,-,-,-
+625,70TSU/FRI,4394942.0,10.1016/S0021-9258(18)62643-2,,['eng'],245,22,5914-26,The Journal of biological chemistry,-,Nov 1970,"Y Tsuda, H C Friedmann"
+626,70VEE/RAI,4315932.0,10.1042/bj1170499,,['eng'],117,3,499-503,The Biochemical journal,"1. The ratio [ATP]/[ADP][P(i)], as measured by direct determination of the three components in rat liver, was found in various nutritional states to have approximately the same value as the ratio [ATP]/[ADP][P(i)] calculated from the concentrations of lactate, pyruvate, glyceraldehyde phosphate and 3-phosphoglycerate on the assumption that lactate dehydrogenase, glyceraldehyde phosphate dehydrogenase and 3-phosphoglycerate kinase are at near-equilibrium in the liver. This implies that the redox state of the NAD couple in the cytoplasm is linked to, and partially controlled by, the phosphorylation state of the adenine nucleotides. 2. The combined equilibrium constant of the glyceraldehyde 3-phosphate dehydrogenase and 3-phosphoglycerate kinase reactions at 38 degrees C and I0.25, was found to be 5.9x10(-6). 3. The fall of the [NAD(+)]/[NADH] ratio in starvation and other situations is taken to be the consequence of a primary fall of the [ATP]/[ADP][HPO(4) (2-)] ratio.",Apr 1970,"R L Veech, L Raijman, H A Krebs"
+627,70WUR/HES,4395302.0,10.1515/bchm2.1970.351.2.1537,,['eng'],351,12,1537-44,Hoppe-Seyler's Zeitschrift fur physiologische Chemie,-,Dec 1970,"B Wurster, B Hess"
+628,70WUR/SCH,5451283.0,10.1515/bchm2.1970.351.2.961,,['ger'],351,8,961-6,Hoppe-Seyler's Zeitschrift fur physiologische Chemie,-,Aug 1970,"B Wurster, F Schneider"
+629,71BRI/CAR,5168977.0,10.1021/bi00800a028,,['eng'],10,24,4522-33,Biochemistry,-,Nov 1971,"H G Britton, J Carreras, S Grisolia"
+630,71BRI/CLA,,,,-,-,-,-,-,-,-,-
+631,71CHE/ALI,5095956.0,,,['rus'],36,4,717-22,"Biokhimiia (Moscow, Russia)",-, 1971,"E P Chetverikova, L L Alievskaia, A V Krinskaia"
+632,71COH/WOL,4944312.0,10.1016/S0021-9258(19)45813-4,,['eng'],246,24,7566-8,The Journal of biological chemistry,-,Dec 1971,"R M Cohen, R Wolfenden"
+633,71GLO/POT,,10.1111/j.1471-4159.1971.tb11987.x,,-,-,-,-,-,-,-,-
+634,71HAY/GRE,4328843.0,10.1016/S0021-9258(18)61884-8,,['eng'],246,18,5840-3,The Journal of biological chemistry,-,Sep 1971,"O Hayaishi, P Greengard, S P Colowick"
+635,71HOR/HUS,5148773.0,,,['ger'],27,5,821-37,Acta biologica et medica Germanica,-, 1971,"A Horn, R Husung, M Schröder, H Börnig"
+636,71JEN/SCH,,10.1021/ja00745a017,,-,-,-,-,-,-,-,-
+637,71JOS/WAK,4934182.0,10.1016/0003-9861(71)90234-7,,['eng'],143,2,493-505,Archives of biochemistry and biophysics,-,Apr 1971,"V C Joshi, S J Wakil"
+638,71KAT,4401291.0,10.1016/s0003-9861(71)80057-7,,['eng'],146,1,202-14,Archives of biochemistry and biophysics,-,Sep 1971,S Kato
+639,71KUN/STA,5574401.0,10.1016/S0021-9258(18)62235-5,,['eng'],246,10,3378-88,The Journal of biological chemistry,-,May 1971,"H F Kung, T C Stadtman"
+640,71MCC/CHA,5129727.0,10.1016/S0021-9258(19)45873-0,,['eng'],246,23,7207-13,The Journal of biological chemistry,-,Dec 1971,"J L McCullough, B A Chabner, J R Bertino"
+641,71NOJ/TAN,,10.1093/oxfordjournals.jbchem.a129527,,-,-,-,-,-,-,-,-
+642,71RAJ/LUM,,10.1021/j100680a006,,-,-,-,-,-,-,-,-
+643,71ROB,5570433.0,10.1016/S0021-9258(18)61962-3,,['eng'],246,16,4995-5002,The Journal of biological chemistry,-,Aug 1971,R M Roberts
+644,71RUD/JOH,4322715.0,10.1016/S0021-9258(19)76969-5,,['eng'],246,5,1271-3,The Journal of biological chemistry,-,Mar 1971,"S A Rudolph, E M Johnson, P Greengard"
+645,71SHI/SUG,5552394.0,10.1111/j.1432-1033.1971.tb01312.x,,['eng'],19,2,256-63,European journal of biochemistry,-,Mar 1971,"H Shimono, Y Sugino"
+646,71TAK/KUR,4106365.0,10.1016/S0021-9258(18)61885-X,,['eng'],246,18,5843-5,The Journal of biological chemistry,-,Sep 1971,"K Takai, Y Kurashina, C Suzuki, H Okamoto, A Ueki"
+647,71TAN/JOH,4945184.0,10.1128/jb.108.3.1107-1111.1971,,['eng'],108,3,1107-11,Journal of bacteriology,"Preparations of pyruvate formate-lyase were made from Escherichia coli cells. Net reversal of the ""phosphoroclastic split"" of pyruvate was readily demonstrated with these preparations. Incubation of acetyl phosphate with formate resulted in the accumulation of pyruvate in concentrations up to 0.5 mm. Catalytic amounts of coenzyme A were essential. Pyruvate was also readily formed from acetyl coenzyme A and formate. The equilibrium constant of the reaction (pyruvate(-) + HPO(4) (2-) --> acetyl phosphate(2-) + formate(-)) has been determined to be about 23 at 37 C.",Dec 1971,"N Tanaka, M J Johnson"
+648,71UNK/GOL,5573236.0,10.1016/S0021-9258(18)62300-2,,['eng'],246,8,2354-9,The Journal of biological chemistry,-,Apr 1971,"J C Unkeless, P Goldman"
+649,71WIL/ROC,5580657.0,10.1021/bi00784a017,,['eng'],10,8,1384-90,Biochemistry,-,Apr 1971,"J O Williams, T E Roche, B A McFadden"
+650,71WOH,4398630.0,10.1111/j.1432-1033.1971.tb01503.x,,['eng'],21,4,575-81,European journal of biochemistry,-,Aug 1971,-
+651,72BAK/JEN,4344229.0,10.1016/S0021-9258(19)44584-5,,['eng'],247,23,7724-34,The Journal of biological chemistry,-,Dec 1972,"J J Baker, I Jeng, H A Barker"
+652,72CAG/FRI,4337852.0,10.1016/S0021-9258(19)45152-1,,['eng'],247,11,3382-92,The Journal of biological chemistry,-,Jun 1972,"L M Cagen, H C Friedmann"
+653,72COO/MEI,5059882.0,10.1021/bi00755a001,,['eng'],11,5,661-71,Biochemistry,-,Feb 1972,"J L Cooper, A Meister"
+654,72DAH/AND,5016652.0,10.1016/S0021-9258(19)45519-1,,['eng'],247,7,2238-41,The Journal of biological chemistry,-,Apr 1972,"A S Dahms, R L Anderson"
+655,72DEL,4624446.0,10.1016/S0021-9258(19)45108-9,,['eng'],247,12,3822-8,The Journal of biological chemistry,-,Jun 1972,D P Delmer
+656,72DUF/NEL,5019592.0,10.1111/j.1471-4159.1972.tb01417.x,,['eng'],19,4,959-77,Journal of neurochemistry,-,Apr 1972,"T E Duffy, S R Nelson, O H Lowry"
+657,72FOR/GAU,4335290.0,10.1021/bi00756a026,,['eng'],11,6,1108-14,Biochemistry,-,Mar 1972,"P I Forrester, G M Gaucher"
+658,72GUS/GAN,5012314.0,10.1016/S0021-9258(19)45571-3,,['eng'],247,5,1387-97,The Journal of biological chemistry,-,Mar 1972,"G L Gustafson, J E Gander"
+659,72KHA/ZHE,4660956.0,,,['eng'],6,5,547-52,Molecular biology,-, 1972,"M I Khabarova, S M Zhenodarova"
+660,72KOR/HUR,,10.1016/0005-2744(72)90965-5,,-,-,-,-,-,-,-,-
+661,72LEH/TAN,,10.1016/0076-6879(72)28075-2,,-,-,-,-,-,-,-,-
+662,72MAR/BEL,4623846.0,10.1016/S0021-9258(19)45234-4,,['eng'],247,10,3223-8,The Journal of biological chemistry,-,May 1972,"L R Maréchal, E Belocopitow"
+663,72NAG/JAE,4403556.0,10.1515/bchm2.1972.353.1.773,,['ger'],353,5,773-81,Hoppe-Seyler's Zeitschrift fur physiologische Chemie,-,May 1972,"M Nagelschmidt, L Jaenicke"
+664,72NEL/KIE,5082943.0,10.1016/0003-2697(72)90451-4,,['eng'],49,2,474-8,Analytical biochemistry,-,Oct 1972,"D P Nelson, L A Kiesow"
+665,72ROS/SLA,,10.1016/0005-2728(72)90116-8,,-,-,-,-,-,-,-,-
+666,72STU,5061975.0,10.1016/S0021-9258(19)45701-3,,['eng'],247,3,968-9,The Journal of biological chemistry,-,Feb 1972,J M Sturtevant
+667,72TAK/ONO,,10.1093/oxfordjournals.jbchem.a129946,,-,-,-,-,-,-,-,-
+668,72WOL,,10.1101/SQB.1973.037.01.076,,-,-,-,-,-,-,-,-
+669,72WUR/HES,,10.1016/0014-5793(72)80311-9,,-,-,-,-,-,-,-,-
+670,73BEE/STE,,,,-,-,-,-,-,-,-,-
+671,73DEW/LOW,4697392.0,10.1016/S0021-9258(19)44082-9,,['eng'],248,8,2829-35,The Journal of biological chemistry,-,Apr 1973,"P De Weer, A G Lowe"
+672,73GUY/GEL,4743509.0,10.1016/S0021-9258(19)43346-2,,['eng'],248,20,6957-65,The Journal of biological chemistry,-,Oct 1973,"R W Guynn, H J Gelberg, R L Veech"
+673,73GUY/VEE,4355193.0,10.1016/S0021-9258(19)43347-4,,['eng'],248,20,6966-72,The Journal of biological chemistry,-,Oct 1973,"R W Guynn, R L Veech"
+674,73HAN/RUD,4270771.0,10.1016/S0021-9258(19)43267-5,,['eng'],248,22,7852-9,The Journal of biological chemistry,-,Nov 1973,"R L Hanson, F B Rudolph, H A Lardy"
+675,73HAV/PIT,,10.1007/978-1-4615-8897-9_45,,-,-,-,-,-,-,-,-
+676,73HER,4745770.0,10.1016/S0021-9258(19)43289-4,,['eng'],248,21,7295-303,The Journal of biological chemistry,-,Nov 1973,L B Hersh
+677,73LAN,,10.1007/978-1-4684-6985-1_70,,-,-,-,-,-,-,-,-
+678,73MCC/KOL,,10.1139/o73-069,,-,-,-,-,-,-,-,-
+679,73RAD/HOC,,10.1016/0005-2744(73)90065-X,,-,-,-,-,-,-,-,-
+680,73ROT/KIS,4201495.0,10.1016/S0021-9258(19)43266-3,,['eng'],248,22,7845-51,The Journal of biological chemistry,-,Nov 1973,"S W Rothman, R L Kisliuk, N Langerman"
+681,73SHE/GUL,,,,-,-,-,-,-,-,-,-
+682,73SOM/COS,4711468.0,10.1021/bi00738a008,,['eng'],12,14,2597-604,Biochemistry,-,Jul 1973,"R Somack, R N Costilow"
+683,73STU/GER,,10.1021/ja00805a036,,-,-,-,-,-,-,-,-
+684,73SUG,4719122.0,10.1021/bi00739a014,,['eng'],12,15,2862-8,Biochemistry,-,Jul 1973,T Sugiyama
+685,73SUZ/IWA,,10.1093/oxfordjournals.pcp.a074864,,-,-,-,-,-,-,-,-
+686,73VEL/GUY,4718747.0,10.1016/S0021-9258(19)43738-1,,['eng'],248,13,4811-9,The Journal of biological chemistry,-,Jul 1973,"D Veloso, R W Guynn, M Oskarsson, R L Veech"
+687,73VID/UDE,,10.1016/0005-2744(73)90337-9,,-,-,-,-,-,-,-,-
+688,73WUR/HES,4279207.0,10.1515/bchm2.1973.354.1.407,,['eng'],354,4,407-20,Hoppe-Seyler's Zeitschrift fur physiologische Chemie,-,Apr 1973,"B Wurster, B Hess"
+689,74BEL/MAR,4212162.0,10.1111/j.1432-1033.1974.tb03659.x,,['eng'],46,3,631-7,European journal of biochemistry,-,Aug 1974,"E Belocopitow, L R Maréchal"
+690,74BOS/YAM,4826883.0,10.1021/bi00707a008,,['eng'],13,10,2051-6,Biochemistry,-,May 1974,"R Bose, E W Yamada"
+691,74BUR,4156827.0,10.1042/bj1430365,,['eng'],143,2,365-8,The Biochemical journal,The heat of the reaction NAD(+)+propan-2-ol=NADH+acetone+H(+) was determined to be 42.5+/-0.6kJ/mol (10.17+/-0.15kcal/mol) from equilibrium measurements at 9-42 degrees C catalysed by yeast alcohol dehydrogenase. With the aid of thermochemical data for acetone and propan-2-ol the values of DeltaH=-29.2kJ/mol (-6.99kcal/mol) and DeltaG(0)=22.1kJ/mol (5.28kcal/mol) are derived for the reduction of NAD (NAD(+)+H(2)=NADH+H(+)). These values are consistent with analogous but less accurate data for the ethanol-acetaldehyde reaction. Thermodynamic data for the reduction of NAD and NADP are summarized.,Nov 1974,K Burton
+692,74CHE/PAT,,10.1016/0020-711X(74)90096-2,,-,-,-,-,-,-,-,-
+693,74CLA/BIR,4854821.0,10.1042/bj1390491,,['eng'],139,3,491-7,The Biochemical journal,"The equilibrium constant of the phosphoglyceromutase reaction was determined over a range of pH (5.4-7.9), in solutions of different ionic strength (0.06-0.3) and in the presence of Mg(2+), at 30 degrees C and at 20 degrees C. The values obtained (8.65-11.65) differ substantially from previously published values. The third acid dissociation constants were redetermined for 2- and 3-phosphoglycerate, and in contrast with previous reports the pK values (7.03 and 6.97 respectively at zero ionic strength) were closely similar. The Mg(2+)-binding constants were measured spectrophotometrically and the values, 286mm(-1) and 255mm(-1) for 2- and 3-phosphoglycerate at pH7 and ionic strength 0.02, were also very similar. From the relative lack of effect of temperature, pH and ionic strength it is concluded that the equilibrium constant differs from unity largely because of entropic factors. At low ionic strength, in the neutral region, the pH-dependence can be attributed to the small difference in the acid dissociation constants, but the difference in dissociation constants does not explain the pH-dependence in the acid region or at high ionic strength. Within physiological ranges of pH, Mg(2+) concentration and ionic strength there will be little variation in equilibrium constant.",Jun 1974,"J B Clarke, M Birch, H G Britton"
+694,74DAN/CAR,4548670.0,10.1111/j.1432-1033.1974.tb03763.x,,['eng'],48,1,255-62,European journal of biochemistry,-,Oct 1974,"C Danzin, R Cardinaud"
+695,74FER/STR,4219834.0,10.1042/bj1440477,,['eng'],144,3,477-86,The Biochemical journal,"3-Hexulose phosphate synthase and phospho-3-hexuloisomerase were purified 40- and 150-fold respectively from methane-grown Methylococcus capsulatus. The molecular weights of the enzymes were approximately 310000 and 67000 respectively, as determined by gel filtration. Dissociation of 3-hexulose phosphate synthase into subunits of molecular weight approx. 49000 under conditions of low pH or low ionic strength was observed. Within the range of compounds tested, 3-hexulose phosphate synthase is specific for formaldehyde and d-ribulose 5-phosphate (forward reaction) and d-arabino-3-hexulose 6-phosphate (reverse reaction), and phospho-3-hexuloisomerase is specific for d-arabino-3-hexulose 6-phosphate (forward reaction) and d-fructose 6-phosphate (reverse reaction). A bivalent cation is essential for activity and stability of 3-hexulose phosphate synthase; phospho-3-hexuloisomerase is inhibited by many bivalent cations. The pH optima of the two enzymes are 7.0 and 8.3 respectively and the equilibrium constants are 4.0x10(-5)m and 1.9x10(2)m respectively. The apparent Michaelis constants for 3-hexulose phosphate synthase are: d-ribulose 5-phosphate, 8.3x10(-5)m; formaldehyde, 4.9x10(-4)m; d-arabino-3-hexulose 6-phosphate, 7.5x10(-5)m. The apparent Michaelis constants for phospho-3-hexuloisomerase are: d-arabino-3-hexulose 6-phosphate, 1.0x10(-4)m; d-fructose 6-phosphate, 1.1x10(-3)m.",Dec 1974,"T Ferenci, T Strom, J R Quayle"
+696,74FLO/FLE,,10.1016/S0021-9258(19)42596-9,,-,-,-,-,-,-,-,-
+697,74FRA/LEE,,,,-,-,-,-,-,-,-,-
+698,74GAU/MAI,4150793.0,10.1016/S0021-9258(19)42739-7,,['eng'],249,8,2366-72,The Journal of biological chemistry,-,Apr 1974,"M A Gaunt, U S Maitra, H Ankel"
+699,74GUY/VEL,4374936.0,10.1042/bj1400369,,['eng'],140,3,369-75,The Biochemical journal,"The concentration of cytoplasmic free pyrophosphate was calculated in freeze-clamped livers of rats from the measured concentration of reactants and K(eq.) of the UDP-glucose pyrophosphorylase reaction (UDP-alpha-d-glucose 1-phosphate uridylyltransferase, EC 2.7.7.9). The K(eq.) of the UDP-glucose pyrophosphorylase reaction was redetermined at 38 degrees C, pH7.0, I=0.25mol/l and free [Mg(2+)]=1mm, and was 4.55 in the direction of glucose 1-phosphate formation. The activity of UDP-glucose pyrophosphorylase in rat liver was between 46 and 58mumol of glucose 1-phosphate formed/min per g fresh wt. in the four dietary conditions studied. A fluorimetric assay with enzymic cycling was developed for the measurement of glucose 1-phosphate in HClO(4) extracts of rat liver. The calculated free cytoplasmic PP(i) concentration in nmol/g fresh wt. of liver was 2.3+/-0.3 in starved, 3.8+/-0.4 in fed, 4.9+/-0.6 in meal-fed and 5.2+/-0.4 in sucrose-re-fed animals. These values agree well with recently determined direct measurements of total PP(i) in rat liver and suggest that there is not a large amount of bound or metabolically inert PP(i) in rat liver. The cytoplasmic [ATP]/[AMP][PP(i)] ratio is 10(3) times the cytoplasmic [ATP]/[ADP][P(i)] ratio and varies differently with dietary state. The reaction PP(i)+H(2)O-->2P(i) catalysed by inorganic pyrophosphatase (EC 3.6.1.1) does not attain near-equilibrium in vivo. PP(i) should be considered as one of the group of small inorganic ions which is metabolically active and capable of exerting a controlling function in a number of important metabolic reactions.",Jun 1974,"R W Guynn, D Veloso, J W Lawson, R L Veech"
+700,74GUY/WEB,4275341.0,10.1016/S0021-9258(19)42664-1,,['eng'],249,10,3248-54,The Journal of biological chemistry,-,May 1974,"R W Guynn, L T Webster, R L Veech"
+701,74JEB/TY,4373722.0,10.1073/pnas.71.11.4630,,['eng'],71,11,4630-4,Proceedings of the National Academy of Sciences of the United States of America,"The modified adenine nucleotides ATP-NO, ADP-NO, and AMP-NO were tested as potential substrates and/or inhibitors of mitochondrial phosphotransferases. ADP-NO is not recognized by the translocase system located in the inner mitochondrial membrane; however, it is rapidly phosphorylated to ATP-NO in the outer compartment of mitochondria, by way of the nucleosidediphosphate kinase (EC 2.7.4.6) reaction, provided there is sufficient ATP in the mitochondria. AMP-NO is not phosphorylated by liver mitochondria to the corresponding nucleoside diphosphate; it cannot serve as substrate for adenylate kinase (EC 2.7.4.3). ATP-NO and ADP-NO, however, are substrates of this enzyme. The apparent equilibrium constant for the reaction, ADP-NO + ADP right harpoon over left harpoon ATP-NO + AMP, of 0.908 at pH 7.4 and 5 mM Mg(2+) is significantly higher than that of the reaction with natural nucleotides. Although adenosine N(1)-oxide is easily phosphorylated to AMP-NO by adenosine kinase [Schnebli et al. (1967) J. Biol. Chem. 242, 1997-2004], the formation of corresponding nucleoside triphosphate in vivo seems also to be limited by adenylate kinase; adenosine N(1)-oxide cannot replace adenosine in restoring the normal ATP level in ethionine-treated rats.",Nov 1974,"G Jebeleanu, N G Ty, H H Mantsch, O Bârzu, G Niac, I Abrudan"
+702,74KEN,4831620.0,,,['eng'],160,2,358-65,Archives of biochemistry and biophysics,-,Feb 1974,J Kennedy
+703,74KNA/BLA,4615902.0,10.1111/j.1432-1033.1974.tb03894.x,,['eng'],50,1,253-63,European journal of biochemistry,-,Dec 1974,"J Knappe, H P Blaschkowski, P Gröbner, T Schmitt"
+704,74KUR/TAK,4846750.0,10.1016/S0021-9258(19)42395-8,,['eng'],249,15,4824-8,The Journal of biological chemistry,-,Aug 1974,"Y Kurashina, K Takai, C Suzuki-Hori, H Okamoto, O Hayaishi"
+705,74LAN,,,,-,-,-,-,-,-,-,-
+706,74MCG/PHI,4364415.0,10.1016/S0021-9258(19)42648-3,,['eng'],249,10,3132-9,The Journal of biological chemistry,-,May 1974,"W G McGregor, J Phillips, C H Suelter"
+707,74MCK,,,,-,-,-,-,-,-,-,-
+708,74SCA/SHI,,10.1002/star.19740261202,,-,-,-,-,-,-,-,-
+709,74SCH/STU,,,,-,-,-,-,-,-,-,-
+710,74TUR/GIL,4436332.0,10.1016/S0021-9258(19)81292-9,,['eng'],249,23,7695-700,The Journal of biological chemistry,-,Dec 1974,"R L Turnquist, T A Gillett, R G Hansen"
+711,74UEB/BLA,4217278.0,10.1111/j.1432-1033.1974.tb03780.x,,['eng'],48,2,389-405,European journal of biochemistry,-,Oct 1974,"K H Ueberschär, E O Blachnitzky, G Kurz"
+712,74WON/FRE,4606575.0,10.1021/bi00716a011,,['eng'],13,19,3889-94,Biochemistry,-,Sep 1974,"L J Wong, P A Frey"
+713,75BOH/SCH,241184.0,,,['ger'],34,1,15-20,Acta biologica et medica Germanica,"A calorimetric procedure for determining deltaH, deltaG, deltaS and Keq of a bimolecular reaction with two or more products is described. By using this method the thermodynamic parameters of the phosphofructokinase reaction are determined. At pH 7.0 and 25 degrees C a reaction enthalpy of-6.96kcal/mole was found after correction for the neutralization enthalpy of the buffer and of the enthalpy difference of the magnesium complexes of ATP and ADP, respectively. The free energy of the phosphofructokinase reaction has been found under these conditions to be -3.96kcal/mole.", 1975,"H J Böhme, W Schellenberger, E Hofmann"
+714,75BRA/JAR,1117007.0,10.1016/S0021-9258(19)41718-3,,['eng'],250,6,2315-8,The Journal of biological chemistry,"A 15-dyroxyprostaglandin dehydrogenase has been purified from human placenta to apparent monodispersity. The reaction catalyzed by this enzyme is freely reversible with an equilibrium constant of approximately 6.5 times 10-8 M. The activation energy is 9900 calories per mol. The molecular weight of the enzyme determined by gel filtration is 51,500; sodium dodecyl sulfate disc gel electrophoresis gives a value of 42,000. No evidence was obtained for the existence of multiple forms of the enzyme or for subunits.",Mar 1975,"S S Braithwaite, J Jarabak"
+715,75COH/LYN,,10.1016/0005-2744(75)90324-1,,-,-,-,-,-,-,-,-
+716,75DON/BAR,,10.1016/0040-6031(75)80018-9,,-,-,-,-,-,-,-,-
+717,75GER/WES,168198.0,10.1016/S0021-9258(19)41278-7,,['eng'],250,13,5059-67,The Journal of biological chemistry,"The enthalpies of hydrolysis of acyclic, monocyclic, and glycoside cyclic phosphate diesters have been measured by flow microcalorimetry using a phosphohydrolase isolated from Enterobacter aerogenes as catalyst. The values so obtained (kilocalories per mol) (at 25 degrees) for sodium salts are: diethyl phosphate, minus 1.8 plus or minus 0.5; ethylene phosphate, minus 6.4 plus or minus 0.2; trimethylene phosphate, minus 3.0 plus or minus 0.2; tetramethylene phosphate, minus 2.2 plus or minus 0.1; methyl beta-D-ribofuranoside cyclic 3:5-phosphate, minus 11.1 plus or minus 0.2; methyl alpha-D-glucopyranoside cyclic 4:6-phosphate, minus 6.3 plus or minus 0.1; and cyclic adenosine 3:5-monophosphate (5-ester bond), minus 11.1 plus or minus 0.4 (10-minus 3 M Mg-2+). The enthalpy of hydrolysis of the 3-ester bond of cyclic adenosine 3:5-monophosphate (10-minus 3 M Mg-2+) has been revised to minus 11.1 plus or minus 0.2 kcal/mol from the value of minus 13.2 plus or minus 0.4 kcal/mol reported previously (greengard, p., rudolph, s.a., and sturtevant, j. m. (1969) j. biol. Chem. 244, 4798). All these values pertain to the hydrolysis of singly charged diesters to form singly charged monoesters. The data for the acyclic and monocyclic phosphodiesters are in qualitative agreement with their hydrolytic reactivities. The enthalpies measured for the hydrolysis of the glycoside cyclic phosphates cannot now be explained on the basis of their structures or reactivities; perhaps a contribution to the enthalpies by solvation or a previously unrecognized geometric strain effect may be responsible for the large exothermic enthalpies of these cyclic phosphate diesters. Changes in the heat capacity, increment Cp, for some of the hydrolytic reactions were also measured.",Jul 1975,"J A Gerlt, F H Westheimer, J M Sturtevant"
+718,75GOL,240453.0,10.1016/0301-4622(75)80011-1,,['eng'],3,3,192-205,Biophysical chemistry,-,Jul 1975,R N Goldberg
+719,75GOR/ESF,237482.0,10.1016/0003-9861(75)90274-x,,['eng'],168,2,450-4,Archives of biochemistry and biophysics,-,Jun 1975,"G Gorin, A Esfandi, G B Guthrie"
+720,75GRI/CAR,,10.1016/0076-6879(75)42149-8,,-,-,-,-,-,-,-,-
+721,75IZU/REE,240851.0,10.1016/S0021-9258(19)40819-3,,['eng'],250,20,8085-7,The Journal of biological chemistry,"D-Ribose isomerase, which catalyzes the conversion of D-ribose to D-ribulose, was purified from extracts of Mycobacterium smegmatis grown on D-ribose. The purified enzyme crystalized as hexagonal plates from a 44% solution of ammonium sulfate. The enzyme was homogenous by disc gel electrophoresis and ultracentrifugal analysis. The molecular weight of the enzyme was between 145,000 and 174,000 by sedimentation equilibrium analysis. Its sedimentation constant of 8.7 S indicates it is globular. On the basis of sodium dodecyl sulfate gel electrophoresis in the presence of Mn2+, the enzyme is probably composed of 4 identical subunits of molecular weight about 42,000 to 44,000. The enzyme was specific for sugars having the same configuration as D-ribose at carbon atoms 1 to 3. Thus, the enzyme could also utilize L-lyxose, D-allose, and L-rhamnose as substrates. The Km for D-ribose was 4 mM and for L-lyxose it was 5.3 mM. The enzyme required a divalent cation for activity with optimum activity being shown with Mn2+. the Km for the various cations was as follows: Mn2+, 1 times 10(-7) M, Co2+, 4 times 10(-7) M, and Mg2+, 1.8 times 10(-5) M. The pH optimum for the enzyme was 7.5 to 8.5. Polyols did not inhibit the enzyme to any great extent. The product of the reaction was identified as D-ribulose by thin layer chromatography and by preparation of the O-nitrophenylhydrazone derivative.",Oct 1975,"K Izumori, A W Rees, A D Elbein"
+722,75JEN/NYG,235429.0,10.1111/j.1432-1033.1975.tb03925.x,,['eng'],51,1,253-65,European journal of biochemistry,"The purine nucleoside phosphorylases from Escherichia coli and from Salmonella typhimurium have been purified to electrophoretic homogeneity and crystallized. Comparative studies revealed that the two enzymes are very much alike. They obey simple Michaelis-Menten kinetics for their substrates with the exception of phosphate for which they show negative cooperativity. Gel filtration on Sephadex G-200 of the native enzymes revealed a molecular weight for both enzymes of 138000 plus or minus 10%. By use of dodecylsulphate gel electrophoresis a subunit molecular weight of 23700 plus or minus 5% was determined, suggesting that both enzymes consist of six subunits of equal molecular weight. When the subunits were partially crosslinked with dimethyl suberimidate before dodecylsulphate electrophoresis six protein bands were observed in agreement with the proposed oligomeric state of the enzyme, consisting of six subunits of equal molecular weight. Analysis of the amino acid composition also indicates that the subunits are identical. 6M guanidinium chloride dissociates the enzymes; association experiments with native and succinylated enzymes suggested that only the hexameric form is active. Both enzymes could be dissociated into subunits by p-chloromercuribenzoate; this dissociation is prevented by the substrates: the nucleosides, the pentose 1-phosphates, and mixtures of phosphate and purine bases.",Feb 1975,"K F Jensen, P Nygaard"
+723,75JES,1133398.0,10.1021/ja00840a006,,['eng'],97,7,1662-7,Journal of the American Chemical Society,-,Apr 1975,N D Jespersen
+724,75KAP/BAR,,,,-,-,-,-,-,-,-,-
+725,75KRI,,10.1016/S0076-6879(75)41094-1,,-,-,-,-,-,-,-,-
+726,75KUR/KON,,,,-,-,-,-,-,-,-,-
+727,75MAN/LAN,808172.0,10.1016/0003-9861(75)90324-0,,['eng'],169,1,126-33,Archives of biochemistry and biophysics,-,Jul 1975,"A Mangold, N Langerman"
+728,75MCC/JOV,1092683.0,10.1016/S0021-9258(19)41388-4,,['eng'],250,11,4073-80,The Journal of biological chemistry,"A steady state kinetic study of Escherichia coli DNA polymerase I has been carried out using poly[d(A-T)] as the template-primer substrate. The results of substrate saturation and product inhibition kinetic studies suggest an altered Ordered Bi Bi mechanism for the enzyme. The Michaelis constants for polymer, d-atp, and dTTP are 5 nM (3'-OH ends), 1 muM, and 2 muM, respectively. The apparent equilibrium constant for the reaction, Keq equals [PPi]/[dNTP], was estimated as greater than or equal to 500. No quaternary complex of enzyme, template, and both deoxynucleoside triphosphates was detected. Single turnover experiments at 4 degrees indicated that the enzyme functions non-processively under the specified conditions, that is, dissociates after each catalytic step. The results at higher temperature were consistent with dissociation within 30 steps. Furthermore, at 4 degrees a burst of incorporation stoichiometric with the amount of enzyme was observed upon initiation of the reaction, indicating that the rate-limiting step in the steady state occurs after phosphodiester bond formation. There is a linear Arrhenius dependence of the initial reaction on temperature in the range 4-40 degrees, with an apparent Ea equals 17 kcal/mol. The rate equations appropriate for template-dependent polymerases which dissociate after each catalytic step have been derived.",Jun 1975,"W R McClure, T M Jovin"
+729,75MCG/JOR,,10.1021/ac60356a048,,-,-,-,-,-,-,-,-
+730,75MUR/TSU,,10.1016/0005-2744(75)90040-6,,-,-,-,-,-,-,-,-
+731,75PIE/GUY,237900.0,10.1016/S0021-9258(19)41323-9,,['eng'],250,12,4445-50,The Journal of biological chemistry,"The observed equilibrium constant (Kobs) for the reaction of choline acetyltransferase (EC 2.3.1.6) has been determined under physiological conditions. Using sigma and square brackets to indicate total concentrations of all ionic species present: (see article). The value of Kobs has been determined to be 12.3 plus or minus 0.6 at 38 degrees, pH 7.0 and ionic strength 0.25 M. The value at 25 degrees is not significantly different, and the constant has been found to be insensitive to variations in ionic strength (0.03 to 0.375 M), pH (6.5 TO 7.5) OR FREE [Mg-2+] (0 to 5 mM). The Kobs of this reaction reflects the difference between the observed standard free energy change (delta G-oobs) for the hydrolysis of acetylcholine and the delta G-oobs for the hydrolysis of acetyl-CoA. Since the delta G-oobs for the hydrolysis of acetyl-CoA has been previously determined to be minus 8.54 kcal/mol (minus 35.75 kJ/mol under the same physiological conditions, the delta G-oobs for the reaction of acetylcholinesterase (EC 3.1.1.7): (SEE ARTICLE). Can be calculated to be minus 6.99 kcal/mol (minus 29.26 kJ/mol) at pH ionic strength 0.25 M and 38 degrees, taking the standard state of liquid water to have unit activity ([H2O] equals 1). The pKa for acetic acid under the same conditions, has been determined to be 4.60 plus or minus 0.01, allowing the Kobs for the pH-independent reaction (see article). To be calculated to be 3.28 times 10-2 M. Choline and carnitine are chemical analogues. The Kobs for the corresponding reaction of carnitine acetyltransferase (EC 2.3.1.7). (SEE ARTICLE). Under the same physiological conditions of pH (7.0), ionic strength (0.25 M), and temperature (38 degrees) has been determined to be 1.73 plus or minus 0.05, making the delta G-oobs for the hydrolysis of acetylcholine only 1.21 kcal/mol (5.06 kJ) less negative than that for the hydrolysis of acetylcarnitine.",Jun 1975,"J R Pieklik, R W Guynn"
+732,75SCH/GRE,170102.0,10.1111/j.1432-1033.1975.tb02227.x,,['eng'],56,1,245-52,European journal of biochemistry,"The enzyme system prostaglandin 15-hydroxy dehydrogenase, which catalyzes the inactivation of all biologically active prostaglandins, has been purified 1270-fold from human placenta. Kinetic studies on the enzyme have provided information on a well-organized control mechanism to avoid prostaglandin accumulation and for a fast prostaglandin degradation. 15-Ketoprostaglandin E2 and 13,14-dihydro-15-ketoprostaglandin E2 inhibit prostaglandin 15-hydroxy dehydrogenase non-competitively with respect to prostaglandin E2. The rate equation of enzyme reaction for two substrates was used for determination of the equilibrium constant and Michaelis constants of the enzyme. The following kinetic constants for prostaglandin 15-hydroxy dehydrogenase have been found. The equilibrium constant with repect to prostaglandin E2 is 18 muM, the Michaelis constant Km for prostaglandin E2 is 1 muM for NAD+ 44muM. The inhibition constants for 15-ketoprostaglandin E2 ar Ki(slope) = 70 muM, Ki(intercept) = 150 muM, and for 13,14-dihydro-15-ketoprostaglandin E2 Ki(slope) = 80 muM, and Ki(intercept) = 150 muM. The maximal velocity for the forward reaction is V1 = 0.45 mumol/min. These kinetic data exclude a random or ping-pong mechanism, and also a Theorell-Chance type as suggested by Braithwaite and Jarabak. We propose, therefore, a sequential ordered mechanism. The isoelectric point for prostaglandin 15-hydroxy dehydrogenase is at pH 5.35, judged by isoelectric focusing.",Aug 1975,"W Schlegel, R O Greep"
+733,75SCH/RIF,1191642.0,10.1021/bi00695a020,,['eng'],14,24,5347-54,Biochemistry,"When malic enzyme is added to a mixture of malate-2-d, TPN, CO2, pyruvate, and TPNH at concentrations calculated to be at equilibrium, the TPNH level first drops and then increases slowly to its original level. This equilibrium perturbation is caused by slower cleavage of C-D than C-H bonds during hydride transfer as malate-2-d and TPNH are partly converted into TPND and malate-2-h in the process of establishing isotopic equilibrium. With malate-2-d, isotope effects for malic enzyme at pH 7.1 and malate dehydrogenase at pH 9.3 of 1.45 and 1.70-2.16 (depending on oxaloacetate level) were determined with this method, while the corresponding isotope effects on V/Kmalate and V for the chemical reactions were 1.5-1.8 and 1.0, and 1.9 and 1.5 for the two enzymes. The advantage of this method is its extreme sensitivity, and the lack of interference from various artifacts. The sensitivity is sufficient to permit determination of 13C and 15N isotope effects in favorable cases, and values of 1.031 for malic enzyme with 13CO2, and 1.047 for glutamate dehydrogenase with 15NH4+ have been determined. In the course of this work it was discovered that the equilibrium constants for oxidation by DPN, and oxidative decarboxylation by TPN are lower for malate-2-d than for malate-2-h by a factor of 0.76-0.82. Changes in Keq upon deuterium substitution, which are predicted by the calculations of Hartshorn and Shiner (1972), should be observed for many other reactions as well.",Dec 1975,"M I Schimerlik, J E Rife, W W Cleland"
+734,75SHI/BEA,169260.0,10.1016/S0021-9258(19)41016-8,,['eng'],250,17,6891-6,The Journal of biological chemistry,"Using a homogeneous enzyme from rabbit skeletal muscle, it has been demonstrated that the cyclic adenosine 3':5'-monophosphate (cyclic AMP)-dependent protein kinase reaction is reversible. In addition to the phosphorylated protein substrate, the reverse reaction requires Mg2+, ADP, and cyclic AMP when the holoenzyme is used as the source of enzyme. It is independent of cyclic AMP when the catalytic subunit of the protein kinase is used. The optimum pH for the reverse reaction with 32P-labeled casein as the substrate is 5.7, essentially the same as that for the forward reaction. Among the nucleotide subtrates tested, ADP serves as the best phosphoryl group acceptor. The Km of the enzyme for ADP is 3.3 mM and that for 32P-casein is 1.7 mg/ml. The equilibrium constant at 30 degrees is approximately 0.042 at a magnesium concentration of 10 mM and a pH of 6.9. This result indicates that the free energy of hydrolysis (deltaG0obs) of the phosphorylated protein substrate is relatively high, i.e. approximately -6.5 kcal/mol under these conditions.",Sep 1975,"Y Shizuta, J A Beavo, P J Bechtel, F Hofmann, E G Krebs"
+735,75SUN,241749.0,10.1016/S0021-9258(19)40710-2,,['eng'],250,22,8585-90,The Journal of biological chemistry,"Ethanolaminephosphate cytidylyltransferase (EC 2.7.7.14), which catalyzes a central step in phosphatidylethanolamine synthesis, has been purified 1000-fold from a postmicrosomal supernatant from rat liver. The enzyme, which requires a reducing agent, like dithiothreitol, for activity, is stable for weeks at 0-4 degrees when stored in the presence of dithiothreitol and in the pH range 7.5 to 9.0. A molecular weight of 100 to 120 X 10(3) was estimated by gel chromatography on Sephadex G-200. Gel electrophoresis in the presence of sodium dodecyl sulfate gave only one protein band with an apparent molecular weight of 49 to 50 X 10(3). The reaction catalyzed by the enzyme is reversible with a Keq for the forward reaction of 0.46 under the assay conditions. Michaelis constants of 53 and 65 muM were determined for CTP and ethanolaminephosphate, respectively. From the product inhibition pattern an ordered sequential reaction mechanism is proposed, in which CTP is the first substrate to add to the enzyme and CDP-ethanolamine is the last product to be released. The possible role of this reaction in the regulation of phosphatidylethanolamine synthesis in liver is discussed.",Nov 1975,R Sundler
+736,75WYR/GRI,1250.0,10.1111/j.1432-1033.1975.tb02418.x,,['eng'],59,1,9-15,European journal of biochemistry,"Two isoenzymes of an NADP+ -dependent cinnamyl alcohol dehydrogenase and an NAD+ - dependent aliphatic alcohol dehydrogenase were extracted from cell suspension cultures of soybean (Glycine max L., var. Mandarin) which form lignin during growth. These enzymes could be separated from each other by chromatography on DEAE-cellulose and hydroxyapatite. The cinnamyl alcohol dehydrogenase isoenzymes were partially purified by (NH4)2SO4 fractionation, and column chromatography on DEAE-cellulose, Sephadex G-100, and hydroxyapatite. The molecular weight of the enzymes were estimated by the elution volumes from a Sephadex G-100 column and were found to be about 43,000 (isoenzyme 1) and 69,000 (isoenzyme 2). Maximum rates of reaction were observed in the case of coniferyl alcohol oxidation at pH 9.2 (Isoenzyme 1) and pH 8.8 (isoenzyme 2); in the reverse reaction pH 6.5 was optimal for isoenzyme 2. Whereas isoenzyme 1 is specific for coniferyl alcohol, isoenzyme 2 can also oxidize cinnamyl alcohol and a number of substituted cinnamyl alcohols, Km values for substituted cinnamaldehydes are 3-11 times lower than for the corresponding alcohols. Neither isoenzyme reacted with benzyl alcohol, anisic alcohol or ethanol. Substrate inhibition for the forward and reverse reaction was found with isoenzyme 2 but not with isoenzyme 1. The equilibrium constant was determined to be about 10(9) in favour of coniferaldehyde reduction. The possible role of the cinnamyl alcohol dehydrogenase in lignin biosynthesis is discussed.",Nov 1975,"D Wyrambik, H Grisebach"
+737,76BER/KLY,7996.0,,,['rus'],21,6,519-23,Antibiotiki,The equilibrium constant for penicillin amidase-catalyzed hydrolysis of benzylpenicillin(Keg =3.00 +/- 0.24 x 10(-3) M at pH 5.0) and the ionization constants for phenylacetic acid (PAA) and the amino groups of 6-aminopenicillanic acid (6-APA) were determined (4.20 and 4.60 under conditions of the kinetic experiments respectively). The experimental data at pH 6.0 satisfactorily correlated with the theoretical pH-dependence for Keg constructed according to the hypothesis that benzylpenicillin synthesis has a thermodynamic optimum at pH 4.4 equal to a half-sum of the pK values for the carboxylic and amino groups of the PAA and 6-APA respectively.,Jun 1976,"I V Berezin, A A Klesov, A L Margolin, P S Nys, E M Savitskaia"
+738,76CRA/WAI,182134.0,10.1042/bj1550679,,['eng'],155,3,679-87,The Biochemical journal,"1. Isoelectric focusing studies of human placental diamine oxidase showed the pI value of the active enzyme to be 6.5. This information was used in modifying the enzyme purification by incorporating column chromatography on DEAE-Sephadex with ionic strength and pH gradient elution and this, together with affinity chromatography on concanavalin A--Sepharose, gave a highly purified preparation, with a specific activity of 7.0 units/mg. 2. The enzyme gave the expected stoicheiometry with p-dimethylaminomethylbenzylamine as substrate (Keq. 2700) and also oxidized [8-arginine]vasopressin, [8-lysine]vasopressin, collagen and tropocollagen. Polyacrylamide gel slices showed identical migration of diamine-oxidizing and [8-lysine]vasopressin-oxidizing activity. 3. The molecular weight, determined by ultracentrifugation, sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, variable polyacrylamide-gel electrophoresis and Sephadex G-200 column chromatography, was estimated to be approx. 70000. 4. E.s.r. spectroscopy showed that copper and manganese were present in the purified enzyme. This result was confirmed by atomic absorption spectroscopy, which indicated a stoicheiometry for copper and manganese of approx. 1.0 and 1.2g-atom respectively/70000mol.wt. unit. 5. The e.s.r. spectral intensity did not decrease nor did the spectral line shape change when excess of p-dimethylaminomethylbenzylamine was added to the enzyme. 6. Addition of K13CN to the enzyme eliminated the copper e.s.r. signal without affecting the manganese signal. 7. The placental enzyme therefore appears to differ from other amine oxidases in terms of its metal cofactor requirement, molecular weight and substrate specificity, and possible roles in vivo for this enzyme are discussed.",Jun 1976,"M J Crabbe, R D Waight, W G Bardsley, R W Barker, I D Kelly, P F Knowles"
+739,76FAR/CRY,819440.0,10.1016/S0021-9258(17)33309-4,,['eng'],251,14,4389-97,The Journal of biological chemistry,"The kinetic mechanism of ATP sulfurylase was established from initial velocity, product inhibition, and dead-end inhibition studies. In the forward direction, the reaction is steady state ordered, with MgATP=A, sulfate=B, MgPP1=P, and APS=Q.KmA=0.38 mM, Kia=0.71 mM, KmB=0.50 mM. Nitrate and chlorate are competive with sulfate and uncompetitive with MgATP. KiNO3-=0.25 mM; KiC1O3-= 0.15 mM. AMP and various MgATP analogs are competitive with MgATP and mixed-type inhibitors with respect to SO42-. The Ki for AMP is 0.55 mM. The reaction is rapid equilibrium ordered in the reverse direction with Kiq=0.3 to 1.0 muM and Kmp=0.65 muM. Adenosine 5'-phosphosulfate (APS) exhibits competitive substrate inhibition (KIQ=0.3 mM). The ratio Vmaxf/Vmaxr is 0.018. In the forward direction the ratio VmaxMoO42-/VmaxSO42- is 20. The Keq at pH 8.0 and 30 degrees calculated from the Haldane equation is 6 X 10(-9) to 3.3 X 10(-8) (depending on the Kiq value chosen). The experimental Keq is about 2.5 X 10(-9). The fact that Vmax/Vmaxr is about 1 million times greater than Keq is consistent with the assumed physiological role of the enzyme (APS synthesis). The mechanistic basis of the ordered binding sequence was probed by multiple inhibition analysis. Dead-end inhibitors competitive with MgATP (such as free ATP, Mg alpha,beta-methylene ATP, CrATP, and CaATP) do not induce substrate inhibition by sulfate or alter the inhibition patterns displayed by nitrate. This result suggests (but does not prove) that catalytic action on MgATP must precede the formation of the sulfate binding site.",Jul 1976,"J R Farley, D F Cryns, Y H Yang, I H Segel"
+740,76GOL,,10.1016/0301-4622(76)80067-1,,-,-,-,-,-,-,-,-
+741,76GRE/BRI,186026.0,10.1042/bj1570591,,['eng'],157,3,591-8,The Biochemical journal,"The kinetics of the electron-transfer process which occurs between ferrocytochrome c and partially reduced mammalian cytochrome oxidase were studied by the rapid spectrophotometric techniques of stopped flow and temperature jump. Stopped-flow experiments showed initial very fast extinction changes at 605 nm and at 563 nm, indicating the simultaneous reduction of cytochrome a and oxidation of ferrocytochrome c. During this 'burst' phase, say the first 50 ms after mixing, it was invariably found that more cytochrome c had been oxidized than cytochrome a had been reduced. This discrepancy in electron equivalents may be accounted for by the rapid reduction of another redox site in the enzyme, possibly that associated with the extinction changes observed at 830 nm. During the incubation period in which the partially reduced oxidase was prepared, the rate of reduction of cytochrome a by ferrocytochrome c, at constant reactant concentrations, decreased with time. Temperature-jump experiments showed the presence of two relaxation processes. The faster of the two phases was assigned to the electron-transfer reaction between cytochrome c and cytochrome a. A study of the concentration-dependence of the reciprocal relaxation time for this phase yielded a rate constant of 9 X 10(6)M-1-s-1 for the electron transfer from cytochrome c to cytochrome a, and a value of 8.5 X 10(6)M-1-s-1 for the reverse reaction. The equilibrium constant for the electron-transfer reaction is therefore close to unity. The slower phase has been interpreted as signalling the transfer of electrons between cytochrome a and another redox site within the oxidase molecule.",Sep 1976,"C Greenwood, T Brittain"
+742,76GUY,186456.0,10.1016/S0021-9258(17)32957-5,,['eng'],251,22,7162-7,The Journal of biological chemistry,"The observed equilibrium constants (Kobs) of the P-choline hydrolysis reaction have been determined under physiological conditions of temperature (38 degrees) and ionic strength (0.25 M) and physiological ranges of pH and free [Mg2+]. Using sigma and square brackets to indicate total concentrations: (see article.) The value of Kobs has been found to be relatively insensitive to variations in pH and free [Mg2+]. At pH 7.0 and taking the standard state of liquid water to have unit activity ([H2O] = 1), Kobs = 26.6 M at free [Mg2+] = 0 [epsilon G0obs = -2.03 kcal/mol(-8.48 kJ/mol)], 26.8 M at free [Mg2+] = 10(-3) M, and 28.4 M at free [Mg2+] = 10(-2) M. At pH 8.0, Kobs = 18.8 M at free [Mg2+] = 0, 19.2 M at free [Mg2+] = 10(-3), and 22.2 M at free [Mg2+] = 10(-2) M. These values apply only to situations where choline and Pi concentrations are both relatively low (such as the conditions found in most tissues). At higher concentrations of phosphate and choline, the value of Kobs becomes significantly increased since HPO42- complexes choline weakly (association constant = 3.3 M-1). The value of K at 38 degrees and I = 0.25 M is calculated to be 16.4 +/- 0.3 M [epsilonG0 = 1.73 kcal/mol (-7.23 kJ/mol)]. The K for the P-choline hydrolysis reaction has been combined with the K for the ATP hydrolysis reaction determined previously under physiological conditions to calculate a value of 4.95 X 10(-3 M [deltaG0 j.28 kcal/mol (13.7 kJ/mol] for the K of the choline kinase reaction (EC 2.7.1.32), an important step in phospholipid metabolism: (see article.) Likewise, values for Kobs for the choline kinase reaction at 38 degrees, pH 7.0, and I = 0.25 M have been calculated to be 5.76 X 10(4) [deltaG0OBS = -6.77 KCAL/MOL (-28.3 KJ/mol)] at [Mg2+] = 0; 1.24 X 10(4) [deltaG0obs = -5.82 kcal/mol (-24.4 kJ/mol)] at [Mg2+] = 10(-3) M and 8.05 X 10(3) [delta G0obs = -5.56 kcal/mol (-23.3 kJ/mol)] at [Mg2+ = 10(-2) M. Attempts to determine the Kobs of the choline kinase reaction directly were unsuccessful because of the high value of the constant. The results indicate that in contrast to the high deltaG0obs for the hydrolysis of the ester bond of acetylcholine, the deltaG0obs for the hydrolysis of the ester bond of P-choline is quite low, among the lowest known for phosphate ester bonds of biological interest.",Nov 1976,R W Guynn
+743,76HIL/ATT,10346.0,10.1099/00221287-96-1-185,,['eng'],96,1,185-93,Journal of general microbiology,"Phosphoglycerate mutase has been purified from methanol-grown Hyphomicrobium X and Pseudomonas AMI by acid precipitation, heat treatment, ammonium sulphate fractionation, Sephadex G-50 gel filtration and DEAE-cellulose column chromatography. The purification attained using the Hyphomicrobium X extract was 72-fold, and using the Pseudomonas AMI extract, 140-fold. The enzyme purity, as shown by analytical polyacrylamide gel electrophoresis, was 50% from Hyphomicrobium X and 40% from Pseudomonas AMI. The enzyme activity was associated with one band. The purified preparations did not contain detectable amounts of phosphoglycerate kinase, phosphopyruvate hydratase, phosphoglycerate dehydrogenase or glycerate kinase activity. The molecular weight of the enzymic preparation was 32000 +/- 3000. The enzyme from both organisms was stable at low temperatures and, in the presence of 2,3-diphosphoglyceric acid, could withstand exposure to high temperatures. The enzyme from Pseudomonas AMI has a broad pH optimum at 7-0 to 7-6 whilst the enzyme from Hyphomicrobium X has an optimal activity at pH 7-3. The cofactor 2,3-diphosphoglyceric acid was required for maximum enzyme activity and high concentrations of 2-phosphoglyceric acid were inhibitory. The Km values for the Hyphomicrobium X enzyme were: 3-phosphoglyceric acid, 6-0 X 10(-3) M: 2-phosphoglyceric acid, 6-9 X 10(-4) M; 2,3-diphosphoglyceric acid, 8-0 X 10(-6) M; and for the Pseudomonas AMI ENzyme: 3-4 X 10(-3) M, 3-7 X 10(-4) M and 10 X 10(-6) M respectively. The equilibrium constant for the reaction was 11-3 +/- 2-5 in the direction of 2-phosphoglyceric acid to 3-phosphoglyceric acid and 0-09 +/- 0-02 in the reverse direction. The standard free energy for the reaction proceeding from 2-phosphoglyceric acid to 3-phosphoglyceric acid was -5-84 kJ mol(-1) and in the reverse direction +5-81 kJ mol(-1).",Sep 1976,"B Hill, M M Attwood"
+744,76JES,,10.1016/0040-6031(76)80042-1,,-,-,-,-,-,-,-,-
+745,76LAW/GUY,,,,-,-,-,-,-,-,-,-
+746,76LLO/KHA,,,,-,-,-,-,-,-,-,-
+747,76MUR,,10.1093/oxfordjournals.pcp.a075374,,-,-,-,-,-,-,-,-
+748,76RAO/BUT,186451.0,10.1016/S0021-9258(17)32930-7,,['eng'],251,22,6981-6,The Journal of biological chemistry,"The arginine kinase reaction, the reversible transfer of the terminal phosphoryl group of ATP to L-arginine, has been investigated by the technique of 31P NMR at catalytic and stoichiometric concentrations of the enzyme. Three of the four substrates, ATP, ADP, and P-arginine produce easily distinguishable resonances in the 31P NMR spectrum, thus permitting a determination of equilibrium constants from the integrated areas of the resonances. From the linewidths, the exchange rates between reactants and products may be evaluated. At pH 7.25 and a temperature of 12 degrees, the equilibrium constant at catalytic enzyme concentration: Keq = [MgADP] [P-arginine]/[MgATP] [L-arginine], is found to be 0.10 +/- 0.02 and that at stoichiometric enzyme concentration: K'eq = [E-MgADP] [E-P-arginine]/[E-MgATP] [E-arginine] to be 1.56 +/- 0.5. Thus, as the enzyme concentration increased, the production of P-arginine is increasingly favored. From the NMR line shapes in the presence of excess enzyme, the rate of the single step, the transfer of the phosphoryl group on the surface of the enzyme is found to be 192 +/- 15 s-1 in the forward direction, i.e. from E-MgATP, and 154 +/- 15 s-1 in the reverse direction from E-P-argine. At 12 degrees and pH 7.25, the rate of the overall reaction in the forward direction was determined from kinetic measurements to be 19 s-1, an order of magnitude slower than the rate measured by NMR. It can, therefore, be concluded that the interconversion of substrates on the surface of the enzyme is not the rate-determining step in the overal reaction. From the equilibrium constants and other known data the dissociation constant of P-arginine from its enzyme complex can be determined and is found to be 100 muM.",Nov 1976,"B D Rao, D H Buttlaire, M Cohn"
+749,76RUS/MUL,12947.0,10.1111/j.1432-1033.1976.tb11021.x,,['eng'],70,2,325-30,European journal of biochemistry,"The direct reduction of CO2 to formate is catalysed by formate: NAD oxidoreductase in the presence of substrate amounts of NADH. Proof for this reaction is supplied by the detection of a CO2-dependent NADH oxidation, and by the identification of [14c] formate as the product of a NADH-dependent reduction of [14c]carbonate. The enzyme-catalysed CO2 reduction by NADH attains the equilibrium predicted by thermodynamic considerations, a state which is also reached from the formate side. The Michaelis constant for CO2 is about 40 mM indicating the low affinity of the enzyme for this substrate. The corresponding value for formate is 0.1 mM. Under the special conditions employed the enzyme catalyses the formate oxidation about 30 times faster than the CO2 reduction. That CO2 and not HCO3- is the active species in the reduction was shown by comparing the ph dependency of the velocities of the forward and back reactions and by observing the kinetics of CO2 reduction during the simultaneous attainment of the CO2-HCO3- equilibrium.",Nov 1976,"U Ruschig, U Müller, P Willnow, T Höpner"
+750,76SCH/KRI,,10.1016/0005-2744(76)90051-6,,-,-,-,-,-,-,-,-
+751,76SPR/LIM,1276393.0,10.1002/bit.260180504,,['eng'],18,5,633-48,Biotechnology and bioengineering,"Using whole cells containing glucose isomerase, mathematical models for the enzymatic conversion of D-glucose to D-fructose and for the inactivation of the enzyme catalyst have been postulated and verified experimentally. The heat of reaction, the equilibrium constant, and the individual rate constants and their activation energies have been estimated. The model can be used to predict the time course for the enzymatic production of fructose in a batch reactor within the tested experimental range of 40-80 degrees C.",May 1976,"R D Sproull, H C Lim, D R Schneider"
+752,76TRI/PAR,1259718.0,10.1042/bj1530089,,['eng'],153,1,89-91,The Biochemical journal,"A rapid micro-calorimetric method for the simultaneous determination of the Michaelis-Menten parameters and the enthalpy of enzymic reactions is developed. The hydrolysis of 2': 3'-cyclic CMP by ribonuclease A is studied to test the proposed method; values obtained are in good agreement with already published data. Enzymic hydrolysis of yeast RNA, unlike that of cyclic phosphates, is shown to be endothermic. This result is explained by the two-step mechanism of this reaction.",Jan 1976,"M Tribout, S Paredes, J Léonis"
+753,76WEI/KIR,949971.0,10.1111/j.1432-1033.1976.tb10350.x,,['eng'],65,2,365-73,European journal of biochemistry,"The mechanism of indoleglycerol phosphate synthesis from indole and D-glyceraldehyde 3-phosphate catalyzed by tryptophan synthase has been investigated by steady-state kinetic techniques. The equilibrium constant and the progress curves were measured by use of the difference in absorbance between indole and indoleglycerol phosphate. Stopped-flow measurements show that only the non-hydrated form of D-glyceraldehyde 3-phosphate serves as substrate. The product analogue indolepropanol phosphate was used as an inhibitor to discriminate between possible mechanisms. The data agree well with an ordered addition mechanism with D-glyceraldehyde 3-phosphate adding first. Mechanisms involving random addition of substrates or ordered addition with indole adding first can be excluded because indolepropanol phosphate is a competitive inhibitor only towards glyceraldehyde 3-phosphate. The high affinity of tryptophan synthase for indoleglycerol phosphate leads to product inhibition even at small extents of reaction. Glyceraldehyde 3-phosphate combines with the enzyme with an apparent second-order rate constant, which is not diffusion controlled and generates a site with high affinity for indole.",Jun 1976,"W O Weischet, K Kirschner"
+754,77ANN/WAL,,10.1016/0006-291X(77)91392-4,,-,-,-,-,-,-,-,-
+755,77ANT/GIN,36553.0,,,['rus'],11,5,1160-6,Molekuliarnaia biologiia,"The rate constants of the individual steps of the reversible chymotryptic hydrolysis of N-acetyl-L-phenylalanylglycinamide and methyl N-acetyl-L-phenylalaninate have been calculated on the basis of data on the velocity of the exchange between these substrates and products of their hydrolysis at equilibrium and also on the basis of steady-state kinetics of their cleavage. This was done for peptide substrate at pH 5.5, 7.3 and 8.2 and for ester substrate at pH 5.5. The free energy of the formation of intermediate complexes and free energy of activation were calculated. Thus a complete kinetic and thermodynamic description of chymotryptic catalysis of various pH is performed.", 1977,"V K Antonov, L M Ginodman, A G Gurova"
+756,77APP/NAI,201249.0,10.1042/bj1670087,,['eng'],167,1,87-93,The Biochemical journal,"The reversibility of the NAD+ kinase reaction was established, and the kinetic parameters of the rate equation in the reverse direction were determined. The equilibrium constant of the reaction was determined by using the purified pigeon liver enzyme and radioactively labelled nicotinamide nucleotides. The relationship between kinetic parameters of the forward and reverse reactions is in reasonable agreement with the measured equilibrium constant. As expected from the proposed mechanism of action, the enzyme does not catalyse isotope exchange between NAD+ and NADP+ in the absence of ADP and ATP. Although homogeneous as judged by polyacrylamide-gel electrophoresis, the enzyme preparation exhibits ADP/ATP isotope-exchange activity which could not be separated from NAD+ kinase activity, but kinetic evidence suggests that this is probably due to a contaminant.",Oct 1977,"D K Apps, A C Nairn"
+757,77GRI/LOC,,10.1016/S0003-2670(01)93665-7,,-,-,-,-,-,-,-,-
+758,77LAN/GAR,,10.1002/aic.690230102,,-,-,-,-,-,-,-,-
+759,77REH/JAN,,10.1093/clinchem/23.2.195,,-,-,-,-,-,-,-,-
+760,77SCH/CLE,836801.0,10.1021/bi00623a001,,['eng'],16,4,565-70,Biochemistry,"A number of dead-end inhibitors and alternate substrates were examined to gain an understanding of the substrate specificity and mechanism of malic enzyme. Comparison of Ki values for competitive inhibitors suggested that binding of the l-carboxyl of L-malate is by ion pairing with lysine or arginine, while binding of the 4-carboxyl is weaker, and probably of the induced-dipolar type. The 2-hydroxyl hydrogen bonds to a catalytic group, which, when it is protonated, adsorbs the keto form of oxalacetate. Since the only molecule other than L-malate that is oxidized is L-malate-beta-amide, carbon 4 must be trigonal for substrate activity, although a tetrahedral carbon bearing one or two hydroxyl groups gives good binding. Hydroxy groups at carbon 3 contribute to binding, but prevent substrate activity. Hydroxy and ketomalonates are bound more strongly than any of the four carbon acids, suggesting that the latter are bound with some strain. In inhibition studies, pyruvate analogues were competitive vs. pyruvate but noncompetitive vs. malate, while malate analogues were competitive vs. malate and noncompetitive vs. pyruvate. These compounds thus bind to both enzyme-triphosphopyridine nucleotide (E-TPN) and enzyme-reduced triphosphopyridine nucleotide (E-TPNH), but only malate analogues prevent release of TPN, while pyruvate analogues prevent release of TPNH. Ketomalonate and oxalacetate, both of which are slowly reduced by the enzyme in the presence of TPNH and thus must combine in the keto form with E-TPNH,, appear to combine with E-TPN mainly in the gem-diol (or for oxalacetate, also the enol) form. The substrate for the decarboxylation of oxalacetate at pH 4.5 is the keto form.",Feb 1977,"M I Schimerlik, W W Cleland"
+761,77SCH/TAT,836793.0,10.1021/bi00622a011,,['eng'],16,3,410-9,Biochemistry,"Initial velocity patterns in the presence of product and dead-end inhibitors suggest that in reaction 1 the addition of substrates and release of products occur by a sequential random mechanism: L-serine + tetrahydrofolate in equilibrium glycine + 5,10-methylenetetrahydrofolate. This interpretation is supported by equilibrium isotope-exchange studies. The relative maximum rates of exchange of L-serine in equilibrium glycine and L-serine in equilibrium 5,10-methylenetetrahydrofolate in reaction 1 were not inhibited by high levels of substrates. The relative rates of these two exchange reactions were similar but were not identical. These results suggest that the catalytic interconversion and dissociation of substrates are of the same order of magnitude. Reaction 1 represents the transfer of a one-carbon group from the third carbon of L-serine to tetrahydrofolate. Inhibition studies showed that abortive enzyme ternary complexes are formed with L-serine and tetrahydrofolate compounds, which also contain a one-carbon group, e.g., 5-methyltetrahydrofolate and 5,10-methylenetetrahydrofolate. This suggests that the one-carbon binding site can accomodate two one-carbon groups simultaneously without serious steric hindrance.",Feb 1977,"L V Schirch, C M Tatum, S J Benkovic"
+762,77SRA/FRE,18103.0,10.1016/0003-9861(77)90496-9,,['eng'],181,1,178-84,Archives of biochemistry and biophysics,-,May 1977,"S J Sramek, F E Frerman"
+763,77TRA/JON,925000.0,10.1016/S0021-9258(19)75229-6,,['eng'],252,23,8372-81,The Journal of biological chemistry,-,Dec 1977,"T W Traut, M E Jones"
+764,77VEE/KRU,,10.1515/9783110853704-023,,-,-,-,-,-,-,-,-
+765,78CHR/MAT,30336.0,10.1016/0003-2697(78)90745-5,,['eng'],89,1,225-34,Analytical biochemistry,-,Aug 1978,"R I Christopherson, T Matsuura, M E Jones"
+766,78ERB/BUR,28770.0,10.1016/0005-2744(78)90198-5,,['eng'],525,1,45-54,Biochimica et biophysica acta,"A mechanism for the reduction and oxidation of methyl viologen by Clostridium pasteurianum hydrogenase (hydrogen:ferredoxin oxidoreductase, EC 1.12.7.1) is proposed. Double reciprocal plots for methyl viologen reduction and oxidation at pH values 7.0-9.85 are linear, and the plots for reduction and oxidation are intersecting. Such data are consistent with a mechanism in which the H2 and one methyl viologen bind (either in order or randomly) with subsequent reduction and release of the methyl viologen. A second methyl viologen then is bound, reduced and released. Comparison of the calculated Keq' with the Haldane expression in which both methyl viologens react at the same rate show a large difference. This difference indicates that the two methyl viologens react at different rates. Addition of oxidized electron carriers inhibits the hydrogen-deuterium exchange reaction (i.e., the exchange of protons between H2 and 2H2O). CO reversibly inhibits methyl viologen reduction and is competitive vs. H2. O2 acts as an irreversible inhibitor.",Jul 1978,"D L Erbes, R H Burris"
+767,78INF/KIN,,10.1016/0005-2744(78)90135-3,,-,-,-,-,-,-,-,-
+768,78LYN/GUY,204656.0,10.1016/S0021-9258(17)40856-8,,['eng'],253,8,2546-53,The Journal of biological chemistry,-,Apr 1978,"R Lynn, R W Guynn"
+769,78MCG/BRO,,10.1016/0005-2760(78)90010-3,,-,-,-,-,-,-,-,-
+770,78MEE/AKE,639798.0,10.1111/j.1432-1033.1978.tb12183.x,,['eng'],84,2,421-8,European journal of biochemistry,-,Mar 1978,"R van der Meer, T P Akerboom, A K Groen, J M Tager"
+771,78OKA/GEN,,10.5458/jag1972.25.113,,-,-,-,-,-,-,-,-
+772,78RAO/COH,203583.0,10.1016/S0021-9258(17)38123-1,,['eng'],253,4,1149-58,The Journal of biological chemistry,-,Feb 1978,"B D Nageswara Rao, M Cohn, L Noda"
+773,78ROS/DUB,213437.0,10.1016/S0021-9258(17)34332-6,,['eng'],253,23,8583-92,The Journal of biological chemistry,"The steady state kinetics and effects of salts on chicken breast phosphoglycerate mutase have been examined. The enzyme can catalyze three phosphoryl transfer reactions: mutase, bisphosphoglycerate phosphatase, and bisphosphoglycerate synthase. The mutase rate was measured in the favorable direction (Keq = glycerate-3-P/glycerate-2-P approximately equal to 12) using [2T]glycerate-2-P as substrate. The bisphosphoglycerate phosphatase activity was studied in the presence of the activator, glycolate-2-P. The latter is an analog of the glycerate-P's and appears to act as an abortive mutase substrate. The kinetic pattern obtained with both activities is that of a ping-pong mechanism with inhibition by the second substrate occurring at a lower concentration than the Km value for that substrate. The kinetic parameters for the mutase determined in 50 mM N-[tris(hydroxymethyl)methyl-2-amino]ethanesulfonate (TES)/sodium buffer containing 0.1 M KCl, pH 7.5, 25 degrees C are: Km glycerate-2,3-P2, 0.069 micron; Km glycerate-2-P, 14 micron; Km glycerate-3-P approximately 200 micron; Ki glycerate-2-P, 4 micron. The kinetic parameters for the phosphatase reaction in 50 mM triethanolamine/Cl- buffer, pH 7.5, 25 degrees C are: Km glycerate-2,3-P2, 0.065 micron:Km glycolate-2P, 479 micron; Ki glycolate-2-P, 135 micron. The enzyme is sensitive to changes in the ionic environment. Increasing salt concentrations activate the phosphatase in the presence of glycolate-2-P by decreasing the apparent Km of glycerate-2,3-P2. The effects are due to the anionic component and Cl- greater than acetate greater than TES. The same salts are competitive inhibitors with respect to glycolate-2-P. With high levels of KCl that produce a 30-fold decrease in the apparent maximal velocity due to competition with glycolate-2-P, the Km of glycerate-2,3-P2 remains low. These observations lead us to postulate that each monophosphoglycerate substrate has a separate site on the enzyme and that glycerate-2,3-P2 can bind to either site. The binding of anions to one site of the nonphosphorylated enzyme allows an increase in the on and off rates of glycerate-2,3-P2 at the alternate site. Salts inhibit the mutase reaction. The Km of glycerate-2,3-P2 is increased as is that of glycerate-2-P. The effect on the Km of glycerate-2,3-P2 is attributed to an increase in the off rate/on rate ratio for glycerate-2,3-P2. The bisphosphoglycerate synthase reaction is shown to require added glycerate-3-P. The equilibrium between enzyme and glycerate-1,3-P2 is favorable (Kdiss less than or equal 7 X 10(-8) M) and suggests that in the absence of a separate synthase this reaction may have functional significance.",Dec 1978,"Z B Rose, S Dube"
+774,78SUB,623877.0,10.1016/0301-4622(78)85013-3,,['eng'],7,4,375-8,Biophysical chemistry,The enthalpy change for the oxidative deamination of glutamate by NADP+ catalyzed by bovine liver glutamate dehydrogenase has been determined calorimetrically. The deltaH0 values are 64.6 +/- 1.2 kJ/mol and 70.3 +/- 1.2 kJ/mol at 25 and 35 degrees C respectively. The equilibrium constants for the reaction at the two temperatures were determined spectrophotometrically. This enabled the determination of deltaG0 and deltaS0 of the reaction as well. deltaH0 values were also determined for the reaction using an alternative coenzyme and the deuterated substrate.,Jan 1978,S Subramanian
+775,79BYE/SHE,375973.0,10.1021/bi00579a006,,['eng'],18,12,2471-80,Biochemistry,"The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase catalyzes the oxidative phosphorylation of D-glyceraldehyde 3-phosphate. A variety of phosphonates have been shown to substitute for phosphate in this reaction [Gardner, J. H., & Byers, L. D., (1977) J. Biol. Chem. 252, 5925--5927]. The dependence of the logarithm of the equilibrium constant for the reaction on the pKa2 value of the phosphonate is characterized by a Brłnsted coefficient, betaeq, of approximately 1. This represents the sensitivity of the transfer of the phosphoglyceroyl group between the active-site sulfhydryl residue (in the acyl-enzyme intermediate) and the acyl acceptor on the basicity of the acyl acceptor. Molybdate (MoO42-) can also serve as an acyl acceptor in the glyceraldehyde-3-phosphate dehydrogenase catalyzed reaction. The second-order rate constant for the reaction with molybdate is only approximately 12 times lower than the reaction with phosphate even though the pKa2 of molybdate is 3.1 units lower than the pKa2 of phosphate. The immediate product of the molybdate reaction is the acyl molybdate, 1-molybdo-3-phosphoglycerate. The acyl molybdate, like the acyl arsenate (the immediate product of the reaction when arsenate is the acyl acceptor), is kinetically unstable. At pH 7.3 (25 degrees C), the half-life for hydrolysis of the acyl molybdate, or the acyl arsenate, is less than 2.5 s. Thus, hydrolysis of 1-molybdo- and 1-arseno-3-phosphoglycerate is at least 2000 times faster than hydrolysis of 1,3-diphosphoglycerate under the same conditions. Glyceraldehyde-3-phosphate dehydrogenase has a fairly broad specificity for acyl acceptors. Most tetrahedral oxy anions tested are substrates for the enzyme (except SO4(2-) and SeO4(2-)). Tetrahedral monoanions such as ReO4- and GeO(OH)3- are not substrates but do bind to the enzyme. These results suggest the requirement of at least one anionic site on the acyl acceptor required for binding and another anionic group on the acyl receptor required for nucleophilic attack on the acyl enzyme.",Jun 1979,"L D Byers, H S She, A Alayoff"
+776,79COR/CRO,,,,-,-,-,-,-,-,-,-
+777,79COR/LEA,447732.0,10.1016/S0021-9258(18)50399-9,,['eng'],254,14,6522-7,The Journal of biological chemistry,-,Jul 1979,"N W Cornell, M Leadbetter, R L Veech"
+778,79FLE/TAT,,10.1007/BF01732029,,-,-,-,-,-,-,-,-
+779,79GRI/TAN,,10.1016/S0003-2670(01)93222-2,,-,-,-,-,-,-,-,-
+780,79KIM/PET,475389.0,10.1016/0003-9861(79)90327-8,,['eng'],195,1,66-73,Archives of biochemistry and biophysics,-,Jun 1979,"D F Kimball, L Peterson, D J McLoughlin, R G Wolfe"
+781,79LAB/DEB,231463.0,10.1016/S0300-9084(80)80264-1,,['fre'],61,9,1091-4,Biochimie,"A ""Batch"" microcalorimeter is used at 30 degrees C for the study of the hydrolysis of 4-nitro-phenylphenylphosphonate with a calf-intestinal phosphonate esterase, in a tris buffer, pH 8. The yield of enzymatic hydrolysis is estimated by spectrophotometric determination of the p--nitrophenol evolved; we have then calculated the apparent molar enthalph of the reaction. (delta Happ = -72,2 kj. mol-1). Phenylphosphonic acid, the second reaction product, is not transphosphonylated on tris. The second acidity of phenylphosphonic acid was studied at 30 degrees C by sodium hydroxide electrotitration (pKa2 = 7,13) and by ""Flow"" microcalorimetry (delta Hionization = 19,8 kj.mol-1). In the same manner at 30 degrees C, we measured the heat of ionization of p-nitrophenol (delta Hionization = 26,75 kj.mol-1). These findings allow a calculation for the actual heat of hydrolysis of 4-nitro-phenyl-phenylphosphonate (delta Hrho = -29,7 kj.mol-1).", 1979,"M Labadie, J Debord, J C Breton"
+782,79LAW/VEE,36398.0,10.1016/S0021-9258(18)50400-2,,['eng'],254,14,6528-37,The Journal of biological chemistry,"The observed equilibrium constants (Kobs) of the creatine kinase (EC 2.7.3.2), myokinase (EC 2.7.4.3), glucose-6-phosphatase (EC 3.1.3.9), and fructose-1,6-diphosphatase (EC 3.1.3.11) reactions have been determined at 38 degrees C, pH 7.0, ionic strength 0.25, and varying free magnesium concentrations. The equilibrium constant (KCK) for the creatine kinase reaction defined as: KCK = [sigma ATP] [sigma creatine] divided by ([sigma ADP] [sigma creatine-P] [H+]) was measured at 0.25 ionic strength and 38 degrees C and was shown to vary with free [Mg2+]. The value was found to be 3.78 x 10(8) M-1 at free [Mg2+] = 0 and 1.66 x 10(9) M-1 at free [Mg2+] = 10(-3) M. Therefore, at pH 7.0, the value of Kobs, defined as Kobs = KCK[H+] = [sigma ATP] [sigma creatine] divided by ([sigma ADP] [sigma creatine-P] was 37.8 at free [Mg2+] = 0 and 166 at free [Mg2+] = 10(-3) M. The Kobs value for the myokinase reaction, 2 sigma ADP equilibrium sigma AMP + sigma ATP, was found to vary with free [Mg2+], being 0.391 at free [Mg2+] = 0 and 1.05 at free [Mg2+] = 10(-3) M. Taking the standard state of water to have activity equal to 1, the Kobs of glucose-6-P hydrolysis, sigma glucose-6-P + H2O equilibrium sigma glucose + sigma Pi, was found not to vary with free [Mg2+], being 110 M at both free [Mg2+] = 0 and free [Mg2+] = 10(-3) M. The Kobs of fructose-1,6-P2 hydrolysis, sigma fructose-1,6-P2 equilibrium sigma fructose-6-P + sigma Pi, was found to vary with free [Mg2+], being 272 M at free [Mg2+] = 0 and 174 M at free [Mg2+] = 0.89 x 10(-3) M.",Jul 1979,"J W Lawson, R L Veech"
+783,79MCK/TAV,,10.1016/0304-5102(79)85019-1,,-,-,-,-,-,-,-,-
+784,79PIR/LIL,527937.0,10.1515/bchm2.1979.360.2.1693,,['eng'],360,12,1693-702,Hoppe-Seyler's Zeitschrift fur physiologische Chemie,"1) A new enzyme, 2,3-dimethylmalate lyase, was purified from Clostridium barkeri to about 80% homogeneity. Some of the properties of the enzyme are described. 2) It is shown that the 2,3-dimethylmalic acid (m.p. 143 degrees C) described in the literature represents only one racemic pair. This pair is not attacked by 2,3-dimethylmalate lyase. 3) The isolation of both racemic pairs of 2,3-dimethylmalic acid is described. Half of one pair, m.p. 104-106 degrees C, was converted to propionate and pyruvate by 2,3-dimethylmalate lyase. 4) In combination with earlier work performed by E.R. Stadtman and coworkers the results given under points 1--3 establish 2,3-dimethylmalate as an intermediate in the degradation of nicotinic acid by C. barkeri. 5) Experimental evidence indicates the 2,3-dimethylmalate lyase is no acyl-S-enzyme and that it is different in this respect as well as in quaternary structure from the apparently related enzymes citrate lyase and citramalate lyase.",Dec 1979,"P Pirzer, U Lill, H Eggerer"
+785,79RAO/KAY,429312.0,10.1016/S0021-9258(17)30127-8,,['eng'],254,8,2689-96,The Journal of biological chemistry,-,Apr 1979,"B D Nageswara Rao, F J Kayne, M Cohn"
+786,79REK/EGO,,,,-,-,-,-,-,-,-,-
+787,79SCH/HIN,500017.0,10.1515/bchm2.1979.360.2.1497,,['eng'],360,10,1501-4,Hoppe-Seyler's Zeitschrift fur physiologische Chemie,-,Oct 1979,"F X Schmid, H J Hinz"
+788,79VAN,33191.0,10.1002/jcp.1040980106,,['eng'],98,1,41-7,Journal of cellular physiology,"Inosine triphosphate pyrophosphohydrolase from human erythrocytes was purified and characterized. The enzyme is highly specific for ITP and shows optimal activity in glycine buffer pH 9.6 and 50 mM MgCl2. The Km of the enzyme is 1.3 X 10(-4), the Vmax = 1.2 X 10(-9) and the Keq = 3.8 X 10(4). Human erythrocyte ITP pyrophosphohydrolase does not require SH compounds for activation. The enzyme is inhibited by Cd++, Co++, and Ca++ ions and by p-hydroxymercuribenzoate.",Jan 1979,B S Vanderheiden
+789,79VAN/DEB,376783.0,10.1111/j.1471-4159.1979.tb02290.x,,['eng'],32,6,1769-80,Journal of neurochemistry,-,Jun 1979,"J W van der Laan, T de Boer, J Bruinvels"
+790,79VIC/GRE,218950.0,10.1016/S0021-9258(17)30121-7,,['eng'],254,8,2647-55,The Journal of biological chemistry,-,Apr 1979,"J Victor, L B Greenberg, D L Sloan"
+791,80BEY/ROE,,10.1002/bit.260220313,,-,-,-,-,-,-,-,-
+792,80CAM/SGA,6778396.0,10.1016/0003-9861(80)90098-3,,['eng'],205,1,191-7,Archives of biochemistry and biophysics,-,Nov 1980,"M Camici, F Sgarrella, P L Ipata, U Mura"
+793,80CHE/HED,7437498.0,10.1016/0301-4622(80)80041-x,,['eng'],12,1,73-82,Biophysical chemistry,-,Aug 1980,"R L Cheer, G R Hedwig, I D Watson"
+794,80COO/BLA,7000186.0,10.1021/bi00562a023,,['eng'],19,21,4853-8,Biochemistry,"Primary deuterium equilibrium isotope effects for the reaction of five secondary alcohols with nicotinamide adenine dinucleotide (DPN) to give reduced deuterionicotinamide adenine dinucleotide (DPND) (cyclohexanol-1-d, 1.18; 2-propanol-2-d, 1.175; threo-DL-isocitrate-2-d, 1.168; L-malate-2-d, 1.173; L-lactate-2-d, 1.19) are all approximately 1.18, while for a primary alcohol, ethanol, the value is 1.07, for an amino acid, L-glutamate-2-d, it is 1.14, and for a hemiacetal, glucose-1-d, it is 1.28. In each case deuterium becomes enriched in the alcohol, amino acid, or hemiacetal with respect to DPNH (TPNH). beta-Secondary equilibrium isotope effects for reduction of ketones by DPNH (cyclohexanone-2,2,6,6-d4, 0.82; acetone-d6, 0.78; pyruvate-d3, 0.83; alpha-ketoglutarate-3,3-d2 reduced to glutamate, 0.898; oxaloacetate-3,3-d2, 0.877; oxaloacetate-3R-d, 0.945) give an average value of 0.946/D, with deuterium becoming enriched in the alcohol or amino acid with respect to the ketone. For reduction of acetaldehyde-1-d by DPNH, the observed value of 0.953 includes the equilibrium effect on the hydration equilibrium in addition to that on the reduction, and the calculated values for reduction of the free aldehyde and the hydrate are 0.78 and 1.07. For reduction of benzaldehyde-1-d, which is not hydrated, the observed value was 0.79. The secondary equilibrium isotope effect for conversion of DPN-4-d to DPNH is 0.89, with deuterium becoming enriched in DPNH, and, for conversion of fumarate-2,3-d2 to malate, the value is 0.69, with deuterium becoming enriched in L-malate. The equilibrium isotope effect for reaction of cyclohexanol-1-d with DPN is temperature independent over the range 15-35 degrees C.",Oct 1980,"P F Cook, J S Blanchard, W W Cleland"
+795,80ELM/HAS,6243283.0,10.1016/S0021-9258(19)86229-4,,['eng'],255,2,668-75,The Journal of biological chemistry,-,Jan 1980,"M R El-Maghrabi, W S Haston, D A Flockhart, T H Claus, S J Pilkis"
+796,80FUK/OBO,6987227.0,10.1016/S0021-9258(19)85794-0,,['eng'],255,7,2705-7,The Journal of biological chemistry,"Uridine diphosphoglucose 4-epimerase (EC 5.1.3.2) of Saccharomyces cerevisiae was purified to homogeneity with a yield of 30%. The purification procedure involved ammonium sulfate precipitation, streptomycin treatment, chromatography on diethylaminoethyl cellulose and hydroxylapatite, and Bio-Gel A-0.5m gel filtration. With the purified enzyme preparation, Km and Vmax values for uridine diphosphogalactose were determined and found to be 0.22 mM and 1.26 mmol/h/mg of protein, respectively. The value of Vmax corresponds to a turnover rate of 3890 molecules of uridine diphosphogalactose converted to uridine diphosphoglucose/min/enzyme molecule. The pH optimum of the enzyme was found to be between 6.8 and 8.0. Amino acid analysis was carried out on the final preparation. Based on the result, the partial specific volume was calculated to be 0.74 ml/g. The NH2-terminal residue of the enzyme was studied by two different methods and found to be threonine. The molecular weight and subunit composition were determined by the combination of the sucrose density gradient centrifugation and gel filtration under nondissociating conditions, and by polyacrylamide gel electrophoresis under dissociating conditions. The results indicated that the enzyme has a molecular weight of 183,000, consisting of two identical subunits. Each molecule of the native enzyme contained 1 molecule of NAD+.",Apr 1980,"T Fukasawa, K Obonai, T Segawa, Y Nogi"
+797,80GER/GUT,,10.1021/ja00525a033,,-,-,-,-,-,-,-,-
+798,80JAF/COH,6988421.0,10.1016/S0021-9258(19)85684-3,,['eng'],255,8,3240-1,The Journal of biological chemistry,"It has been demonstrated that the reaction of ATP beta S and 3-P-glycerate catalyzed by 3-P-glycerate kinase, unlike the reaction with ATP, can form a readily detectable amount of 1,3-bis-P-glycerate as observed by 31P NMR. By quantifying production of 1,3-bis-P-glycerate from the phosphorothioate analogue of ATP as a function of time as the reaction approaches equilibrium, Keq for the reaction was estimated to be approximately 400, about 1 order of magnitude less than the equilibrium constant previously reported for the analogous reaction of the normal nucleotide substrates.",Apr 1980,"E K Jaffe, M Cohn"
+799,80LER/COH,6997302.0,10.1016/S0021-9258(18)43565-X,,['eng'],255,18,8756-60,The Journal of biological chemistry,"31P NMR measurements have been found to be a convenient means for simultaneously measuring the concentrations of several species in the equilibrium mixtures of the reactions catalyzed by arginine kinase and creatine kinase. MgATP + X in equilibrium MgADP + XP where X = arginine or creatine and XP = P-arginine or P-creatine. The free energy of phosphorylaton of various metabolites by adenosine 5'-O-(2-thiotriphosphate) at pH 8.0 and 30 degrees C is more exergonic than the corresponding phosphorylations by ATP by about 2.5 kcal/mol, resulting in a displacement of the equilibrium toward the nucleoside diphosphates by a factor of approximately 60. Since this factor does not depend on the nature of the metabolite, the equilibrium constants of thionucleotide reactions may be used to determined the equilibrium constants of corresponding oxynucleotide reactions which lie too far toward ATP. The equilibrium constants of the oxynucleotide reactions catalyzed by pyruvate kinase and 3-P-glycerate kinase calculated by this method from the experimentally determined equilibrium constants of the corresponding thionucleotide reactions are 3.1 x 10(-4) and 2.9 x 10(-4), respectively, under the experimental conditions used. The equilibrium constants and degree of stereoselectivity of the arginine kinase reaction are altered when Ca2+ replaces Mg2+ as the activating metal ion.",Sep 1980,"C L Lerman, M Cohn"
+800,80PET/AMI,,10.1016/0305-0491(80)90077-2,,-,-,-,-,-,-,-,-
+801,80REK/EGO,,,,-,-,-,-,-,-,-,-
+802,80SLI/BOL,,10.1021/ja00540a025,,-,-,-,-,-,-,-,-
+803,80SVE/GAL,,,,-,-,-,-,-,-,-,-
+804,80SVE/MAR,,10.1016/0141-0229(80)90070-8,,-,-,-,-,-,-,-,-
+805,80TER/RAB,7388069.0,,,['rus'],45,2,299-304,"Biokhimiia (Moscow, Russia)","The values of Km and V, pH optimum and thermal stability of urease were determined. It was shown that urease can be effectively used for the study of equilibrium of synthesis and hydrolysis of carbamide under conditions of carbamide in the ammonium carbonate--carbamide--water system at 20 degrees and 37 degrees were determined. The equilibrium constants for carbamide synthesis at the given temperatures were calculated.",Feb 1980,"T P Terekhina, N S Rabovskaia"
+806,81GON/CHE,16345717.0,10.1128/aem.41.2.430-436.1981,,['eng'],41,2,430-6,Applied and environmental microbiology,"d-Xylulose, an intermediate of d-xylose catabolism, was observed to be fermentable to ethanol and carbon dioxide in a yield of greater than 80% by yeasts (including industrial bakers' yeast) under fermentative conditions. This conversion appears to be carried out by many yeasts known for d-glucose fermentation. In some yeasts, xylitol, in addition to ethanol, was produced from d-xylulose. Fermenting yeasts are also able to produce ethanol from d-xylose when d-xylose isomerizing enzyme is present. The results indicate that ethanol could be produced from d-xylose in a yield of greater than 80% by a two-step process. First, d-xylose is converted to d-xylulose by xylose isomerase. d-Xylulose is then fermented to ethanol by yeasts.",Feb 1981,"C S Gong, L F Chen, M C Flickinger, L C Chiang, G T Tsao"
+807,81GRI/CLE,6794611.0,10.1021/bi00523a002,,['eng'],20,20,5650-5,Biochemistry,"L-Alanine dehydrogenase from Bacillus subtilis has a predominately ordered kinetic mechanism in which NAD adds before L-alanine, and ammonia, pyruvate, and NADH are released in that order. When pyruvate is varied at pH 9.35, levels of ammonia above 50 mM cause uncompetitive substrate inhibition and cause the slope replot to go through the origin. This pattern suggest that iminopyruvate (2% of pyruvate at this pH with 150 mM ammonia) can combine with E-NADH much more tightly than pyruvate does but reacts much more slowly because uptake of the required proton from solution is hindered. Isomerization of the initially formed E-NAD complex to a form which can productively bind L-alanine is the slowest step in the forward direction at pH 7.9, and substrate inhibition by L-alanine largely results from combination of the zwitterion in a nonproductive fashion with this initial E-NAD complex, with the result that the isomerization is prevented. All bimolecular rate constants approach diffusion-limited values at optimal states of protonation of enzyme and substrates except that for ammonia, suggesting that ammonia does not form a complex with E-NADH-pyruvate but reacts directly with it to give a bound carbinolamine.",Sep 1981,"C E Grimshaw, W W Cleland"
+808,81HIN/POL,6272654.0,10.1016/0003-9861(81)90344-1,,['eng'],212,1,72-7,Archives of biochemistry and biophysics,-,Nov 1981,"H J Hinz, P Pollwein, R Schmidt, F Zimmermann"
+809,81HIR,16661650.0,10.1104/pp.67.2.221,,['eng'],67,2,221-4,Plant physiology,"To study the role of sorbitol-6-phosphate dehydrogenase in sorbitol synthesis in leaves of Rosaceous plants, properties of the enzyme and its presence in several plants in the family was investigated. The activity of the enzyme, which catalyzes an NADP-dependent oxidation of the substrate to glucose-6-phosphate, was detected in leaves of Prunus mume, Prunus persica, Rhaphiolepsis indica, Sorbus aucuparia, Cydonia oblonga, Photinia glabra, Sorbaria kirilowii, and Spiraea thunbergii.The enzyme was purified about 60-fold from leaves of loquat (Eriobotrya japonica) using affinity chromatography with Blue Sepharose. Neither mannitol-1-phosphate nor fructose-6-phosphate served as substrate. Molecular weight of the enzyme was calculated to be 65,000 at pH 8.0 by gel filtration. Since sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed a peptide of 33,000 daltons, the enzyme was assumed to be a dimer at pH 8.0 K(m) values for sorbitol-6-phosphate, glucose-6-phosphate, NADP, and NADPH were 2.22 millimolar, 11.6 millimolar, 13.5 micromolar, and 1.61 micromolar, respectively. Equilibrium constant for sorbitol-6-phosphate oxidation was 5.12 x 10(-10). Optimal pH for sorbitol-6-phosphate oxidation was 9.8. The enzyme showed its maximum activity within a broad pH range between 7 and 9 for glucose-6-phosphate reduction. The enzyme was more effective in the direction of glucose-6-phosphate reduction than in the reverse direction at neutral pH. Thus, it is suggested that the enzyme catalyzes sorbitol synthesis from glucose-6-phosphate during photosynthesis in leaves of Rosaceous plants.",Feb 1981,M Hirai
+810,81HSI/SU,,,,-,-,-,-,-,-,-,-
+811,81KIS/NIE,7030216.0,10.1016/0003-9861(81)90496-3,,['eng'],211,2,613-21,Archives of biochemistry and biophysics,-,Oct 1981,"R C Kiser, W G Niehaus"
+812,81MER/MCA,7198894.0,10.1016/0003-9861(81)90416-1,,['eng'],212,2,717-29,Archives of biochemistry and biophysics,-,Dec 1981,"D K Merrill, J C McAlexander, R W Guynn"
+813,81PAH/JAG,,10.1016/S0044-328X(81)80048-7,,-,-,-,-,-,-,-,-
+814,81RAM/PIC,,10.1139/m81-164,,-,-,-,-,-,-,-,-
+815,81RAO/COH,7462219.0,10.1016/S0021-9258(19)69866-2,,['eng'],256,4,1716-21,The Journal of biological chemistry,"The reaction catalyzed by rabbit muscle creatine kinase ATP + creatine in equilibrium ADP + P-creatine has been investigated by 31P NMR. At pH 8.0 and 4 degrees C, the equilibrium constant of the overall reaction [P1][P2]/[S1] [S2] is found to be 0.08, while that for the interconversion step between enzyme-bound substrates and products [E.P1. P2]/[E.S1.S2] is estimated to be approximately 1; the latter value is the same for all other kinases investigated. The rate of interconversion of enzyme-bound substrates and products is approximately 90 s-1 and is not the rate-limiting step of the overall reaction. Of the phosphate groups in enzyme complexes of reactants or products, the 31P chemical shifts of beta-P(ADP) and beta-P[MgADP) change by approximately 2 ppm downfield while all others change by less than 0.8 ppm. In the transition state analog complexes E.MgADP.NO3-.creatine and E.MgADP.HCOO-.creatine, the beta-P(MgADP) signal shows a substantial upfield shift in the direction of the beta-P(MgATP) resonance. The pattern of chemical shifts and line shapes of nucleotide complexes of creatine kinase parallel those for the corresponding complexes of arginine kinase, indicating structural and/or conformational similarity of the phosphate chains of nucleotides bound to the two enzymes. However, a difference in active sites is indicated by the pH independence (pH 6.0 to 9.0) of the chemical shift of the beta-P of MgADP bound to creatine kinase, whereas with arginine kinase this resonance showed a pKa approximately 7.5.",Feb 1981,"B D Nageswara Rao, M Cohn"
+816,81SUG/VEI,7197134.0,,,['eng'],53,1,183-93,Anais da Academia Brasileira de Ciencias,"Pullularia pullulans grown on D-xylose induces the synthesis of a xylitol dehydrogenase capable of oxidizing xylitol to D-xylulose in the presence of NAD according to the following reaction: Xylitol + NAD+ in equilibrium to D-xylulose + NADH + H+. Cells grown on D-glucose do not show appreciably xylitol dehydrogenase activity. However, synthesis of the enzyme begins when those cells were transferred to a liquid medium containing D-xylose. This evidence suggests that xylitol dehydrogenase is an induced enzyme. The purified xylitol dehydrogenase of Pullularia pullulans is quite specific for xylitol, unlike similar dehydrogenases from other sources, which attack a variety of polyols of variable chain length. This property makes the enzyme useful for the determination of xylitol, even in the presence of other polyols.",Mar 1981,"J K Sugai, L A Veiga"
+817,82BAR/HEB,,10.1016/0076-6879(82)83045-0,,-,-,-,-,-,-,-,-
+818,82DEM,,10.1111/j.1749-6632.1982.tb25773.x,,-,-,-,-,-,-,-,-
+819,82GAL/SVE,,10.1016/0167-4838(82)90242-4,,-,-,-,-,-,-,-,-
+820,82GUY,6293382.0,10.1016/0003-9861(82)90315-0,,['eng'],218,1,14-25,Archives of biochemistry and biophysics,-,Oct 1982,R W Guynn
+821,82GUY/THA,6284052.0,10.1016/0003-9861(82)90110-2,,['eng'],215,2,514-23,Archives of biochemistry and biophysics,-,May 1982,"R W Guynn, H Thames"
+822,82HSI/CHI,,10.1016/0141-0229(82)90006-0,,-,-,-,-,-,-,-,-
+823,82NG/WON,7076619.0,10.1128/JB.150.3.1252-1258.1982,,['eng'],150,3,1252-8,Journal of bacteriology,"Oxaloacetate decarboxylase was purified to 136-fold from the oral anaerobe Veillonella parvula. The purified enzyme was substantially free of contaminating enzymes or proteins. Maximum activity of the enzyme was exhibited at pH 7.0 for both carboxylation and decarboxylation. At this pH, the Km values for oxaloacetate and Mg2+ were at 0.06 and 0.17 mM, respectively, whereas the Km values for pyruvate, CO2, and Mg2+ were 3.3, 1.74, and 1.85 mM, respectively. Hyperbolic kinetics were observed with all of the aforementioned compounds. The Keq' was 2.13 X 10(-3) mM-1 favoring the decarboxylation of oxaloacetate. In the carboxylation step, avidin, acetyl coenzyme A, biotin, and coenzyme A were not required. ADP and NADH had no effect on either the carboxylation or decarboxylation step, but ATP inhibited the carboxylation step competitively and the decarboxylation step noncompetitively. These types of inhibition fitted well with the overall lactate metabolism of the non-carbohydrate-fermenting anaerobe.",Jun 1982,"S K Ng, M Wong, I R Hamilton"
+824,82RED,,,,-,-,-,-,-,-,-,-
+825,82REH/YOU,,10.1093/clinchem/28.11.2235,,-,-,-,-,-,-,-,-
+826,82SAL/GIA,,10.1007/BF01959737,,-,-,-,-,-,-,-,-
+827,82SAL/JOR,6812503.0,10.1016/0003-9861(82)90487-8,,['eng'],217,1,139-43,Archives of biochemistry and biophysics,-,Aug 1982,"S J Salamone, F Jordan, R R Jordan"
+828,82SUE/KAT,,10.1016/0304-4165(82)90178-7,,-,-,-,-,-,-,-,-
+829,83BRA,,,,-,-,-,-,-,-,-,-
+830,83CRA/BOS,,10.1016/0003-9861(83)90213-8,,-,-,-,-,-,-,-,-
+831,83HAA/KAR,18551488.0,10.1002/bit.260250715,,['eng'],25,7,1873-95,Biotechnology and bioengineering,"An immobilized Penicillin-V-acylase (commercial name, Novozym 217) with high specificity for the phenoxyacetyl-(V)- side chain was investigated in a recycle reactor and in a batch reactor to find the enzymatic reaction rate as a function of conversion, x, substrate concentration, c(A) (0) and pH. The reaction rate depends strongly on pH, and both products, phenoxy-acetic acid and 6-APA, inhibit the reaction. Nonspecific side reactions amount to only a few per cent when c(A) (0) <150 mM and pH& gt; 6.5. The effectiveness factor for commercial-size particles is found to be about 0.65, and a value of 1.3mM is obtained for the equilibrium constant, K(eq), of the deacylation reaction. A kinetic model for the deacylation process which includes the effect of pH and of the reverse (acylation) reaction is proposed. Rate data for particles of different size are fitted to the nonlinear model. Five kinetic parameters and an effective diffusivity for the immobilized enzyme particles are determined.",Jul 1983,"P Haagensen, L G Karlsen, J Petersen, J Villadsen"
+832,83HON/HAR,,10.1093/oxfordjournals.pcp.a076514,,-,-,-,-,-,-,-,-
+833,83KAT/SUE,6370350.0,,,['jpn'],12,2,173-8,Josai Shika Daigaku kiyo. The Bulletin of the Josai Dental University,-, 1983,"S Katoh, T Sueoka"
+834,83KHO/KAR,,,,-,-,-,-,-,-,-,-
+835,83MIL/RYC,6852021.0,10.1111/j.1432-1033.1983.tb07443.x,,['eng'],133,1,169-72,European journal of biochemistry,"The alpha beta-methylene analogues of ATP and ADP, [alpha beta CH2]ATP and [alpha beta CH2]ADP, are substrates for creatine kinase. However, the rate of the phosphoryl transfer reaction catalysed is about 10(-5)-times lower than that with normal ATP. The affinities of the analogues (especially [alpha beta CH2]ADP) for the enzyme are lower than those of the normal substrates. The equilibrium constant at 25 degrees C, measured using 31P NMR, for the reaction Mg[alpha beta CH2]ATP + creatine in equilibrium Mg[alpha beta CH2]ADP + phosphocreatine + H+ is 2.2 X 10(-12) M compared with a value of 2.5 X 10(-10) M for the same reaction with the normal substrates, corresponding to a difference in delta G0 values of 11.7 kJ X mol-1. It follows that delta G0 for the hydrolysis of the terminal phosphate group of Mg[alpha beta CH2]ATP is less favourable by 11.7 kJ X mol-1 than that for MgATP.",Jun 1983,"E J Milner-White, D S Rycroft"
+836,83PIL/HAN,6885800.0,10.1016/S0021-9258(17)44524-8,,['eng'],258,17,10774-8,The Journal of biological chemistry,"UDP-glucose 4-epimerase and UDP-N-acetylglucosamine 4-epimerase have been co-purified about 9,000-fold from porcine submaxillary glands by affinity chromatography on UDP-hexanolamine-agarose. The homogeneous epimerase has apparent Mr = 88,000 and contains two subunit species with apparent Mr = 37,000 and 35,000, respectively. The two subunits, however, are indistinguishable as judged by peptide mapping. The purified enzyme catalyzes equally well the reversible reactions UDP-glucose in equilibrium UDP-galactose and UDP-N-acetylglucosamine in equilibrium UDP-N-acetylgalactosamine. At saturating substrate concentrations, the ratio of the rate of the former reaction to that of the latter is 1.13 in the forward direction and 0.44 in the backward direction. Both reactions have the same Keq = 0.38 and the same dependence on pH. Moreover, both activities are lost at about the same rate by heat denaturation of the epimerase or reaction with N-ethylmaleimide. Kinetic analysis reveals that the reactants for one reaction are competitive inhibitors of the other reaction, with the Ki values of the inhibitors essentially identical with their Km values as substrates. Taken together, these studies suggest that UDP-glucose 4-epimerase and UDP-N-acetylglucosamine 4-epimerase activities reside in a single enzyme.",Sep 1983,"F Piller, M H Hanlon, R L Hill"
+837,83SEL/MAN,6863314.0,10.1016/S0021-9258(18)32137-9,,['eng'],258,14,8872-5,The Journal of biological chemistry,"Glyoxalase I catalyzes the formation of S-D-lactoyl-glutathione via the hemimercaptal adduct of methylglyoxal and glutathione. This enzymatic reaction, which has been considered virtually irreversible, was found to be reversible under such conditions that glutathione liberated from the thiolester was trapped. The reverse reaction could be monitored spectrophotometrically by use of 5,5'-dithiobis-(2-nitrobenzoate). In addition to 5,5'-dithiobis-(2-nitrobenzoate), 2,2'-dithiobispyridine and cystamine were used to promote the reverse reaction. S-D-Lactoylglutathione did not hydrolyze in the presence of glyoxalase I under the conditions investigated, as shown by its stability in the absence of thioltrapping agents. Proof of the reversal of the reaction was obtained by demonstrating the formation of stoichiometric amounts of methylglyoxal and glutathione from S-D-lactoylglutathione. Catalysis of the reverse reaction was dependent upon the presence of a bivalent metal ion in the active site of the enzyme. Apoenzyme, obtained by removal of the essential Zn2+ from the active site, did not catalyze the reverse reaction, but catalytic activity was restored by addition of Zn2+, Mg2+, Mn2+, or Co2+. The reverse reaction was also catalyzed by glyoxalase I from yeast. Linear competitive inhibition (Ki = 0.64 mM) was obtained with 5,5'-dithiobis-(2-nitrobenzoate), which necessitated correction of the apparent kinetic parameters of the reverse reaction. The corrected values for the reverse reaction catalyzed by glyoxalase I from human erythrocytes with S-D-lactoylglutathione as substrate were kcat = 3.6 s-1 and Km = 1.9 mM. Combination of these values with the corresponding parameters for the forward reaction allowed calculation, through the Haldane relation, of the equilibrium constant, Keq = 1.1 X 10(4), for the isomerization between the hemimercaptal of methylglyoxal and glutathione and S-D-lactoylglutathione. The strong reversible competitive inhibitor of the forward reaction, S-p-bromobenzylglutathione, also inhibited the reverse reaction competitively (Ki = 0.38 microM).",Jul 1983,"S Sellin, B Mannervik"
+838,83TIL,,,,-,-,-,-,-,-,-,-
+839,83VIT/HUA,6357095.0,10.1016/0003-9861(83)90339-9,,['eng'],226,2,687-92,Archives of biochemistry and biophysics,"Using a highly purified enzyme preparation of uridine phosphorylase from Escherichia coli B, we have performed detailed kinetic studies which include initial-velocity and product-inhibition experiments in the forward and reverse directions of the reaction. These studies indicate a rapid-equilibrium random mechanism for this enzyme with the formation of an enzyme . uracil phosphate abortive complex. Lack of formation of the enzyme . uridine . ribose-1-phosphate abortive complex suggests that the ribosyl moiety of the two ligands compete for the same binding site. The random mechanism is different from the ordered addition of substrates found for uridine phosphorylase from other sources. All the kinetic constants in the forward and reverse directions and the Keq of reaction for E. coli uridine phosphorylase are reported herein.",Oct 1983,"A Vita, C Y Huang, G Magni"
+840,83WED/BLA,16663114.0,10.1104/pp.72.4.1021,,['eng'],72,4,1021-8,Plant physiology,"The NAD malic enzyme has been purified to near homogeneity from the leaves of Crassula argentea Thunb. The enzyme has two subunits, one of 59,000 daltons, and one of 62,000 daltons. In native gels stained for activity, the enzyme appears to exist in the dimeric, tetrameric, and predominantly the octameric forms.The enzyme uses either Mg(2+) or Mn(2+) as the required divalent cation, and utilizes NADP at a rate less than 20% of that with NAD. With Mn(2+) the K(m) for malate(2-) is lower than with Mg(2+), but V(max) is lower than with Mg(2+). In the forward (malate-decarboxylating) direction with NAD, the kinetic parameters are essentially like those observed for the enzyme from C(3) plants. In the reverse reaction, run with Mn(2+), the activity is 1.5% of that in the forward reaction. The equilibrium constant is 1.1 x 10(-3) molar.The kinetic mechanism of the reaction, at least in the forward direction, is sequential, with apparently random binding of all reaction components. Product inhibition patterns confirm this.The enzyme displays a strong hysteretic lag, which is shortened by high enzyme concentrations, high substrate concentrations, and the presence of the product NADH.The enzyme is activated by coenzyme A with K(a) = 4 micromolar. AMP also shows competitive activation, with K(a) = 24 micromolar. The activation by coenzyme A and AMP is additive, implying separate sites for their binding. Phosphoenolpyruvate activates the reaction at low (micromolar) concentrations, but higher concentrations of phosphoenolpyruvate cause deactivation. Fumarate(2-) is a strong activator, with K(a) = 0.3 millimolar. Fructose-1,6-bisphosphate activates the enzyme, but its most pronounced effect is in shortening the lag. Citrate is a competitive inhibitor of malate, with K(i) = 4.9 millimolar.",Aug 1983,"R T Wedding, M K Black"
+841,83YAM/SAI,6822536.0,10.1016/S0021-9258(18)33062-X,,['eng'],258,3,1826-32,The Journal of biological chemistry,"NADP-dependent formate dehydrogenase (NADP+) (EC 1.2.1.43) from Clostridium thermoaceticum has been purified to a specific activity of about 1100 mumol min-1 mg-1 when assayed at 55 degrees C and pH 7.5. The enzyme is extremely oxygen-sensitive and 7.6 microM of O2 causes 50% inhibition of initial velocity under assay conditions. Purification was done in an atmosphere at 95% N2 and 5% H2 and by including azide, dithionite, and glycerol as stabilizing agents in all buffer solutions. The enzyme contains, in molar ratios, 2 tungsten, 2 selenium, 36 iron, and about 50 inorganic sulfur. It has a molecular weight of about 340,000 and consist of two each of two different subunits giving the composition alpha 2 beta 2. The molecular weight of the alpha-subunit is 96,000 and that of the beta-subunit is 76,000. The selenium resides in the two alpha-subunits. Tungsten is released from the protein on denaturation and may exist as a tungsten cofactor. The enzyme catalyzes a reduction of CO2 with NADPH at pH 7.5 and 55 degrees C and Keq at these conditions is (2.35 +/- 0.49) x 10(-2) if CO2 is considered the active species and (1.48 +/- 0.31) x 10(-3) if HCO3- is the active species.",Feb 1983,"I Yamamoto, T Saiki, S M Liu, L G Ljungdahl"
+842,84ADA/UED,18551697.0,10.1002/bit.260260203,,['eng'],26,2,121-7,Biotechnology and bioengineering,"A kinetic model was devised for the hydrolysis and synthesis of maltose and isomaltose by two glucoamylases from Rhizopus niveus and Aspergillus niger, and the validity of the model was verified experimentally at 313 K and pH 5.0. For both enzymes, the formations of maltose and isomaltose from glucose were parallel reversible reactions, and glucosyl transfer between maltose and isomaltose was not observed. The enzymes catalyzed rapid hydrolysis and synthesis of maltose. Isomaltose was hydrolyzed and synthesized more slowly, but the level produced from glucose was much higher than that of maltose. These hydrolysis and condensation reactions were expressed well by the model.",Feb 1984,"S Adachi, Y Ueda, K Hashimoto"
+843,84BER/COO,6091737.0,10.1021/bi00313a014,,['eng'],23,18,4101-8,Biochemistry,"Inorganic pyrophosphate dependent D-fructose-6-phosphate 1-phosphotransferase from Propionibacterium freudenreichii was purified to apparent homogeneity by the criterion of silver staining on sodium dodecyl sulfate (SDS) gels. In the direction of phosphorylation of fructose 6-phosphate (F6P), an intersecting initial velocity pattern is obtained when MgPPi is varied at several levels of F6P. In the reverse reaction direction, the reactants are Mg2+, Pi, and fructose 1,6-bisphosphate (FDP). Variation of Pi at several levels of Mg2+ and a single level of FDP gives an intersecting pattern. When this pattern is repeated at several additional FDP levels, data are consistent with a fully random terreactant mechanism at pH 8.0 and 25 degrees C. The Keq calculated from the Haldane relationship [(5 +/- 1.5) X 10(-3) M] agrees with that determined directly from 31P NMR of the equilibrium mixture [(7 +/- 2) X 10(-3) M]. Product inhibition by Pi is competitive vs. either MgPPi or F6P with the other reactant saturating but changes to noncompetitive inhibition when the fixed reactant is decreased to Km levels. Product inhibition by MgPPi is competitive vs. either Pi or FDP with the other reactant saturating but changes to noncompetitive when the fixed reactant is decreased to Km levels. Tagatose 6-phosphate is competitive vs. F6P and noncompetitive vs. MgPPi. Methylenediphosphonate is competitive vs. MgPPi and noncompetitive vs. F6P. Sulfate is competitive vs. Pi and noncompetitive vs. FDP, while 2,5-anhydro-D-mannitol 1,6-bisphosphate is competitive vs. FDP and noncompetitive vs. Pi.",Aug 1984,"B L Bertagnolli, P F Cook"
+844,84BLA/COC,6433972.0,10.1021/bi00306a009,,['eng'],23,11,2377-83,Biochemistry,"Degradation of 7,8-dihydrofolate (H2folate) in the presence of dihydrofolate reductase (DHFR) has been shown due not to an oxygenase activity of the reductase as previously reported but to dismutation of H2folate to folate and 5,6,7,8-tetrahydrofolate (H4folate). The reaction can be followed spectrophotometrically or by analysis of the reaction mixture by high-performance liquid chromatography (HPLC). The products have also been isolated and characterized. Oxygen uptake during the reaction is much less than stoichiometric with H2folate disappearance and is attributed to autoxidation of the H4folate formed. The dismutation activity is a property of highly purified Streptococcus faecium DHFR isoenzyme 2 (but not isoenzyme 1) and of Lactobacillus casei DHFR, but not of bovine liver DHFR. The activity is dependent on tightly bound NADP+ and/or NADPH. Removal of the nucleotide results in loss of dismutation activity, which is restored by adding NADP+ or NADPH. Maximum activity is obtained when approximately 1 mol equiv of nucleotide is added per mol of DHFR. It is proposed that in the dismutation reaction bound NADP(H) is alternately reduced and oxidized by incoming molecules of H2folate with release of folate and H4folate, respectively. The relatively slow rate of folate formation presumably limits the rate of the overall reaction. The equilibrium constant for the dismutation reaction is 19.4 +/- 7.4 at 22 degrees C and pH 7.0. Calculation of standard oxidation-reduction potentials at pH 7 gave values of -0.230 V for the H2folate/H4 folate pair and -0.268 V for the folate/H2folate pair. The mechanism by which NADP+ is retained by the enzyme from some sources during purification procedures is unclear.(ABSTRACT TRUNCATED AT 250 WORDS)",May 1984,"R L Blakley, L Cocco"
+845,84DEM,,10.1016/S0021-9258(20)82109-7,,-,-,-,-,-,-,-,-
+846,84DEY,,10.1016/S0031-9422(00)85013-X,,-,-,-,-,-,-,-,-
+847,84DIT/KUB,,10.1139/m84-214,,-,-,-,-,-,-,-,-
+848,84DIT/KUB2,,10.1111/j.1574-6968.1984.tb01455.x,,-,-,-,-,-,-,-,-
+849,84KOL/EGG,6489933.0,10.1515/bchm2.1984.365.2.847,,['eng'],365,8,847-57,Hoppe-Seyler's Zeitschrift fur physiologische Chemie,"The partial enrichment of a new enzyme, dimethylmaleate hydratase from Clostridium barkeri and some of its characteristics are described. The unstable and oxygen-sensitive hydratase depends on ferrous ions and is induced during growth of C. barkeri on nicotinic acid. The enzyme uses both dimethylmaleate and the hydration product, 2,3-dimethylmalate, as substrates to establish an equilibrium that is 70% in favour of the latter acid; dimethylfumarate is not attacked. A 2,3-dimethyl[3-3H]malate specimen was prepared from dimethylmaleate with the hydratase in tritiated water. Based on proton attack at the re-face of the double bond, experimental results indicate the (2R,3S)-configuration for this malate. The hydration reaction takes an anti-course. The tritium label was lost in the sequence (2R,3S)-2,3-dimethyl[3-3H]malate----(R)-[2-3H1]-propionate----(2R) - [2-3H1]propionyl-CoA----(2S)-methylmalonyl-CoA. This result confirms the stereochemical course of the 2,3-dimethylmalate lyase reaction, inversion of configuration, by an independent approach. The hydratase reaction completes the degradation scheme of nicotinic acid by C. barkeri. The pathway is briefly reviewed.",Aug 1984,"A Kollmann-Koch, H Eggerer"
+850,84LLO/CHA,,,,-,-,-,-,-,-,-,-
+851,84OYA/IRI,,,,-,-,-,-,-,-,-,-
+852,84PAU,,,,-,-,-,-,-,-,-,-
+853,84PUZ/GOR,,,,-,-,-,-,-,-,-,-
+854,84RAG/LJU,6608524.0,10.1016/S0021-9258(17)43122-X,,['eng'],259,6,3499-503,The Journal of biological chemistry,"An NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase has been purified to homogeneity from autotrophically and heterotrophically grown cells of Acetobacterium woodii. The enzymes from the differently grown cells were indistinguishable by gel filtration and sodium dodecyl sulfate electrophoresis and have a final specific activity of 670 units mg-1. The enzyme is oxygen-labile; therefore, it was isolated under anaerobic conditions in the presence of dithiothreitol. The oxidized enzyme can be reactivated with 5 mM dithiothreitol, the half-time of activation being 19 min. The forward and reverse reaction initial velocity kinetics was studied and the enzyme was found to follow a substituted (ping-pong) reaction mechanism. With this model, the Km values for NAD and 5,10-methylenetetrahydrofolate are 4.0 and 0.26 mM, while for NADH and 5,10-methenyltetrahydrofolate, they are 2.0 and 1.0 mM, respectively. The equilibrium constant at pH 6.7, determined by the Haldane relationship, is approximately equal to 2.0, favoring the formation of NADH and 5,10-methenyltetrahydrofolate. The purified enzyme is a Mr = 55,000 dimer which lacks 10-formyltetrahydrofolate synthetase and 5,10-methenyltetrahydrofolate cyclohydrolase activities. At pH 6.7, the conversion of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate occurs at a rate of 98,600 mol min-1 mol-1 of enzyme, while the reverse reaction occurs at a rate of 95,600 mol min-1 mol-1 of enzyme.",Mar 1984,"S W Ragsdale, L G Ljungdahl"
+855,84REK/RUM,,10.1016/0040-6031(84)85121-7,,-,-,-,-,-,-,-,-
+856,84REK/RUM2,,,,-,-,-,-,-,-,-,-
+857,84TEW/GOL,,10.1007/BF00647222,,-,-,-,-,-,-,-,-
+858,84UCH/TSU,6389524.0,10.1093/oxfordjournals.jbchem.a134863,,['eng'],96,2,507-22,Journal of biochemistry,"N-Acetylneuraminate lyase [N-acetylneuraminic acid aldolase EC 4.1.3.3] from Escherichia coli was purified by protamine sulfate treatment, fractionation with ammonium sulfate, column chromatography on DEAE-Sephacel, gel filtration on Ultrogel AcA 44, and preparative polyacrylamide gel electrophoresis. The purified enzyme preparation was homogeneous on analytical polyacrylamide gel electrophoresis, and was free from contaminating enzymes including NADH oxidase and NADH dehydrogenase. The enzyme catalyzed the cleavage of N-acetylneuraminic acid to N-acetylmannosamine and pyruvate in a reversible reaction. Both cleavage and synthesis of N-acetylneuraminic acid had the same pH optimum around 7.7. The enzyme was stable between pH 6.0 to 9.0, and was thermostable up to 60 degrees C. The thermal stability increased up to 75 degrees C in the presence of pyruvate. No metal ion was required for the enzyme activity, but heavy metal ions such as Ag+ and Hg2+ were potent inhibitors. Oxidizing agents such as N-bromosuccinimide, iodine, and hydrogen peroxide, and SH-inhibitors such as p-chloromercuribenzoic acid and mercuric chloride were also potent inhibitors. The Km values for N-acetylneuraminic acid and N-glycolylneuraminic acid were 3.6 mM and 4.3 mM, respectively. Pyruvate inhibited the cleavage reaction competitively; Ki was calculated to be 1.0 mM. In the condensation reaction, N-acetylglucosamine, N-acetylgalactosamine, glucosamine, and galactosamine could not replace N-acetylmannosamine as substrate, and phosphoenolpyruvate, lactate, beta-hydroxypyruvate, and other pyruvate derivatives could not replace pyruvate as substrate. The molecular weight of the native enzyme was estimated to be 98,000 by gel filtration methods. After denaturation in sodium dodecyl sulfate or in 6 M guanidine-HCl, the molecular weight was reduced to 33,000, indicating the existence of 3 identical subunits. The enzyme could be used for the enzymatic determination of sialic acid; reaction conditions were devised for determining the bound form of sialic acid by coupling neuraminidase from Arthrobacter ureafaciens, lactate dehydrogenase, and NADH.",Aug 1984,"Y Uchida, Y Tsukada, T Sugimori"
+859,84WAS/DAU,6391537.0,10.1021/bi00317a015,,['eng'],23,22,5182-7,Biochemistry,"The alanine racemase encoded by the Salmonella typhimurium dadB gene was purified to 90% homogeneity from an overproducing strain. At 37 degrees C the enzyme has a specific activity of 1400 units/mg (V max, L- to D-alanine). Active enzyme molecules are monomers of Mr 39 000 with one molecule of pyridoxal 5'-phosphate bound per subunit. The Km's for L- and D-alanine are 8.2 and 2.1 mM, respectively. Measurement of turnover numbers yielded the expected Keq value of 1.0. Determination of 22 of the 25 N-terminal amino acid residues of the purified polypeptide allowed localization of cloned DNA encoding the structural gene. Sequencing of subcloned DNA revealed that the dadB gene encodes a polypeptide of 356 amino acids whose calculated molecular weight (apoenzyme) was 39 044.",Oct 1984,"S A Wasserman, E Daub, P Grisafi, D Botstein, C T Walsh"
+860,85ANS/PRI,,10.1042/bst0130362,,-,-,-,-,-,-,-,-
+861,85BAD/WAL,3921052.0,10.1021/bi00327a010,,['eng'],24,6,1333-41,Biochemistry,"An alanine racemase has been purified some 30 000-fold almost to homogeneity from Gram-positive Streptococcus faecalis NCIB 6459; the enzyme has been purified to the same extent (4000-fold) from an O-carbamyl-D-serine-resistant mutant with a 7-fold higher enzyme level in crude extract. The racemase has one pyridoxal phosphate molecule per 42-kDa subunit, has a Vmax of 3570 units/mg and a Km of 7.8 mM in the L to D direction, and has a Vmax of 1210 units/mg and a Km of 2.2 mM in the D to L direction. The Keq is 0.8 and kcat/Km values are ca. 3 X 10(5) M-1 s-1. The purified enzyme is inhibited in a time-dependent manner by both L- and D-(l-aminoethyl)phosphonates (Ala-P), confirming observations of Atherton et al. in crude extracts of this organism [Atherton, F. R., Hall, M. J., Hassal, C. H., Holmes, S. W., Lambert, R. W., Lloyd, W. J., & Ringrose, P. S. (1980) Antimicrob. Agents Chemother. 18, 897]. Studies with [1-2H]-, [1-3H]-, and [1,2-14C]Ala-P rule out enzymic activation and processing as the basis for irreversible inhibition. Thus, enzyme after exposure to [14C]Ala-P or [alpha-3H]Ala-P and gel filtration contains stoichiometric amounts of radioactive label, but denaturation quantitatively releases intact Ala-P into solution as revealed by high-performance liquid chromatography and cocrystallization with authentic material. The Ala-P isomers are slow binding inhibitors of this racemase as is the alpha,alpha'-dimethyl analogue but not the D or L isomers of the corresponding phosphinate.(ABSTRACT TRUNCATED AT 250 WORDS)",Mar 1985,"B Badet, C Walsh"
+862,85BAR,16664543.0,10.1104/pp.79.4.1127,,['eng'],79,4,1127-8,Plant physiology,The equilibrium constant for the reaction catalyzed by sucrose phosphate synthase was reported 25 years ago to be 3250 at pH 7.5. It has been redetermined and found to be about 2 in the direction of synthesis and 6 to 10 when measured in the opposite direction.,Dec 1985,G A Barber
+863,85COO/PRA,3966792.0,10.1016/0003-9861(85)90602-2,,['eng'],236,1,26-35,Archives of biochemistry and biophysics,"The ability of 0.4 M KCl to extract over 80% of a short-chain beta-hydroxyacyl-CoA dehydrase from rat hepatic endoplasmic reticulum, while more than 80% of the long-chain beta-hydroxyacyl-CoA dehydrase component of the fatty acid chain elongation system remains intact, confirms the existence of more than one hepatic microsomal dehydrase. Following extraction from the microsomal membrane, the short-chain dehydrase undergoes, at least, a two-fold activation. Employing even-numbered trans-2-enoyl-CoA substrates ranging in carbon chain length from 4 to 16, the highest dehydrase specific activity of 16 mumol min-1 mg protein-1 was obtained with trans-2-hexenoyl-CoA; crotonyl-CoA was the second most active substrate, followed by 8 greater than 10 greater than 12 greater than 14 greater than 16. The specific activity of the short-chain dehydrase with trans-2-hexadecenoyl-CoA (C-16) was only 3% of that observed with the trans-2-hexenoyl-CoA. With crotonyl-CoA or beta-hydroxybutyryl-CoA as substrates, HPLC was employed to identify the products, beta-hydroxybutyryl-CoA, of the hydration reaction, or crotonyl-CoA, of the reverse dehydration reaction. It was also observed that the short-chain dehydrase catalyzed the formation of both D(-) and L(+) stereoisomers of beta-hydroxybutyryl-CoA. The equilibrium constant for the dehydrase-catalyzed reaction determined at pH 7.4 and 35 degrees C, was calculated to be 6.38 X 10(-2) M-1, while the standard free energy change was -775 cal/mol, results similar to those obtained with crystalline crotonase. Finally, based on membrane fraction marker enzymes, substrate specificity, and heat lability of the dehydrase, it was concluded that the microsomal membrane contains a short-chain beta-hydroxyacyl-CoA dehydrase which is separate from the mitochondrial crotonase.",Jan 1985,"L Cook, M R Prasad, R Vieth, D L Cinti"
+864,85DAS/BRO,4092075.0,10.1016/0301-4622(85)80068-5,,['eng'],23,1-2,105-14,Biophysical chemistry,"Direct microcalorimetric measurements were made of the reaction between acetylcholine chloride and acetylcholinesterase (EC 3.1.1.7) that was extracted from electric eel (Electrophorus electricus) and purified by affinity chromatography. Tris-HCl, sodium phosphate and potassium phosphate were used as buffers and sources of ions for the reaction. At pH 7.2 and in 0.1-0.2 M phosphate buffer, the delta H for acetylcholine hydrolysis was found to be -0.107 kcal/mol (under buffered conditions) and -0.931 kcal/mol under unbuffered conditions (water). At pH 8.0 in 0.1 M Tris-HCl buffer, values greater than -2.5 kcal/mol were obtained, with the highest value of -9.2 kcal/mol being seen with bovine erythrocyte acetylcholinesterase. Tris-HCl buffer at 4 X 10(-2) M enhanced the reaction velocity by 51.2% over that of 4 X 10(-3) M buffer. Enzyme purity, pH and ionic milieu of reaction mixture, and substrate concentration affected the measured delta H value.",Nov 1985,"Y T Das, H D Brown, S K Chattopadhyay"
+865,85DEM/BEH,3004566.0,10.1021/bi00347a042,,['eng'],24,26,7783-9,Biochemistry,"The energy of hydrolysis of phosphate compounds varies depending on whether they are in solution or bound to the catalytic site of enzymes. With the purpose of simulating the conditions at the catalytic site, the observed equilibrium constant for pyrophosphate hydrolysis (Kobsd) was measured in aqueous mixtures of dimethyl sulfoxide, ethylene glycol, or polymers of ethylene glycol. The reaction was catalyzed by yeast inorganic pyrophosphatase at 30 degrees C. All the cosolvents used promoted a decrease of Kobsd. Polymers of ethylene glycol were more effective than dimethyl sulfoxide or ethylene glycol in decreasing Kobsd. The higher the molecular weight of the polymer, the lower the value of Kobsd. A decrease in Kobsd from 346 M (delta G degree obsd = -3.5 kcal mol-1) to 0.1 M (delta G degree obsd = 1.3 kcal mol-1) was observed after the addition of 50% (w/v) poly(ethylene glycol) 8000 to a solution containing 0.9 mM MgCl2 and 1 mM Pi at pH 8.0. The association constants of Pi and pyrophosphate for H+ and Mg2+ were measured in presence of different ethylene glycol concentrations in order to calculate the Keq for hydrolysis of different ionic species of pyrophosphate. A decrease in all the Keq was observed. The results are interpreted according to the concept that the energy of hydrolysis of phosphate compounds depends on the different solvation energies of reactants and products.",Dec 1985,"L de Meis, M I Behrens, J H Petretski, M J Politi"
+866,85FAG/DEW,3158649.0,10.1016/S0021-9258(18)88949-9,,['eng'],260,10,6147-52,The Journal of biological chemistry,"The steady state kinetics of calcium transport driven by ATP hydrolysis and ATP synthesis catalyzed by purified, reconstituted calcium ATPase has been investigated as a function of the transmembrane calcium gradient. Purified calcium ATPase was reconstituted into phospholipid vesicles enabling control of the transmembrane calcium gradient. Calcium transport was monitored spectrophotometrically by the calcium indicator, Arsenazo III. Thus, only the enzymatic activity of coupled transport was measured. It was shown under conditions of low external calcium that ATP hydrolysis and synthesis follow simple Michaelis-Menten kinetics and that Michaelis constants obtained for both processes appear independent of the calcium gradient. The maximum velocities for both hydrolysis and synthesis strongly depend on the transmembrane calcium gradient. Based on these results, a mechanism is proposed in which a random addition of substrates for ATP synthesis is followed by random release of ATP and calcium. By measuring the ATP hydrolysis and synthesis under identical conditions, determination of the equilibrium constant for ATP hydrolysis as a function of the transmembrane calcium gradient was possible. Our results indicate that the thermodynamics of the catalytic cycle can be totally accounted for by the energetics of transport of 2.2 +/- 0.3 calciums and the hydrolysis of 1 ATP. An equilibrium constant for ATP hydrolysis in the absence of a calcium gradient was determined to be 4.0 X 10(4).",May 1985,"M H Fagan, T G Dewey"
+867,85GAJ/GOL,4052575.0,10.1016/0301-4622(85)80042-9,,['eng'],22,3,187-95,Biophysical chemistry,"The thermodynamics of the conversion of aqueous fumarate to L-(-)-malate has been investigated using both heat conduction microcalorimetry and a gas chromatographic method for determining equilibrium constants. The reaction was carried out in aqueous Tris-HCl buffer over the pH range 6.3-8.0, the temperature range 25-47 degrees C, and at ionic strengths varying from 0.0005 to 0.62 mol kg-1. Measured enthalpies and equilibrium ratios have been adjusted to zero ionic strength and corrected for ionization effects to obtain the following standard state values for the conversion of aqueous fumarate 2- to malate 2- at 25 degrees C: K = 4.20 +/- 0.05, delta G degrees = -3557 +/- 30 J mol-1, delta H degrees = -15670 +/- 150 J mol-1, and delta C degrees p = -36 +/- J mol-1 K-1. Equations are given which allow one to calculate the combined effects of pH and temperature on equilibrium constants and enthalpies of this reaction.",Aug 1985,"E Gajewski, R N Goldberg, D K Steckler"
+868,85GEU/MAY,3841060.0,10.1111/j.1432-1033.1985.tb09305.x,,['eng'],153,2,327-34,European journal of biochemistry,"The kinetic behaviour of myosin light chain kinase isolated from skeletal muscle was studied under steady-state conditions using highly purified phosphorylatable light chains 2 (LC2). Forward reaction, product inhibition, and reverse reaction data indicate a sequential mechanism which can be interpreted best by a rapid-equilibrium random bi-bi reaction model. The forward reaction parameters are KATP = 150 microM, KLC2 = 5.3 microM, and Ki LC2 = 7.6 microM. The enzyme forms a dead-end complex with ADP and light chain 2; Kd, ADP of this complex is 50 microM. The forward reaction is also strongly inhibited by the phosphorylated light chain 2, Ki, LC2P is 1.5 microM. An equilibrium constant Keq of about 70 can be calculated from the kinetic parameters which agrees with the directly measured value of about 60. The role of the two inhibitory mechanisms in the regulation of the enzyme and of the high energy of the light chain phosphate bond as deducible from Keq are discussed.",Dec 1985,"U Geuss, G W Mayr, L M Heilmeyer"
+869,85HEA/CHU,4066712.0,10.1016/S0021-9258(17)36245-2,,['eng'],260,30,16361-6,The Journal of biological chemistry,"Succinic semialdehyde reductase, a NADP+-dependent enzyme, was purified from whole pig brain homogenates. The enzyme preparation migrates as a single protein and activity band on analytical gel electrophoresis. Succinic semialdehyde reductase (Mr 110,000) catalyzes the reduction of succinic semialdehyde to 4-hydroxybutyrate. The equilibrium constant of the reaction is Keq = 5.8 X 10(7) M-1 at pH 7 and 25 degrees C. The inhibition kinetic patterns obtained when 4-hydroxybutyrate or substrate analogs are used as inhibitors of the reaction catalyzed by the reductase are consistent with an ordered sequential mechanism, in which the coenzyme NADPH adds to the enzyme before the aldehyde substrate. A specific aldehyde reductase was also purified to homogeneity from brain mitochondria preparations. Its catalytic properties are identical to those of the enzyme isolated from whole brain homogenates. It is postulated that two enzymes, i.e. a NAD+-dependent dehydrogenase and a NADP+-dependent reductase, participate in the metabolism of succinic semialdehyde in the mitochondria matrix.",Dec 1985,"W G Hearl, J E Churchich"
+870,85HER/AIY,4052045.0,10.1042/bj2300043,,['eng'],230,1,43-52,The Biochemical journal,"S-Adenosylhomocysteine hydrolase (EC 3.3.1.1) was purified to homogeneity from human placenta by using S-adenosylhomocysteine-agarose affinity chromatography. The enzyme is a tetramer with a native Mr of 189 000 and subunit Mr of 47 000-48 000; there were nine cysteine residues per subunit and no disulphide bonds. The pI was 5.7. H.p.l.c. analysis revealed that the enzyme contained four molecules of tightly bound cofactor (NAD) per tetramer, of which 10-50% was in the reduced form. The enzyme had four binding sites per tetramer for adenosine, of which 10-35% were found to be occupied. Two types of adenosine-binding sites could be distinguished on the basis of differences in rates of dissociation of the enzyme-adenosine complex, and by examining binding of adenosine at 0 degree C and 37 degrees C. The enzyme catalysed the interconversion of adenosine and 4',5'-dehydroadenosine; the equilibrium constant for this reaction was 2.1 and favoured 4',5'-dehydroadenosine formation. Variability in the specific activity of preparations of S-adenosylhomocysteine hydrolase was related to the NAD+/NADH ratio of the preparation. The capacity to bind radioactively labelled adenosine depended on the adenosine content of the purified enzyme. The rate of adenosine binding and the sensitivity of S-adenosylhomocysteine hydrolase to inactivation by adenosine were both diminished in the absence of dithiothreitol.",Aug 1985,"M S Hershfield, V N Aiyar, R Premakumar, W C Small"
+871,85LEE/OSU,2997186.0,10.1016/S0021-9258(17)38662-3,,['eng'],260,26,13909-15,The Journal of biological chemistry,"The diastereomers of adenosine 5'-O-(1-thiotriphosphate) (ATP alpha S), adenosine 5'-O-(2-thiotriphosphate) (ATP beta S), and adenosine 5'-O-(3-thiotriphosphate) (ATP gamma S) could act as substrates for phosphomevalonate kinase in the presence of Mg2+ and Cd2+ as activating divalent metal cations. The Sp diastereomer of ATP alpha S was the preferred substrate regardless of the metal ion used, consistent with the metal ion not binding to the alpha-phosphate. With ATP beta S, the Sp diastereomer was the preferred substrate with Mg2+, and the Rp diastereomer was the preferred substrate with Cd2+. The reversal of specificity establishes that the metal is chelated through the beta-phosphate in the active site of the phosphomevalonate kinase reaction. A comparison of the Vmax values as a function of substitution of oxygen by sulfur showed the order for Mg2+ to be: ATP greater than ATP alpha S(Sp) greater than ATP alpha S(Rp) greater than ATP beta S(Sp) greater than ATP gamma S greater than ATP beta S(Rp). With Cd2+ as the activating metal ion, the order was: ATP greater than ATP alpha S(Sp) greater than ATP alpha S(Rp) greater than ATP beta S(Rp) greater than ATP gamma S greater than ATP beta S(Sp). It is concluded that the chelate structure of metal ATP substrate in the phosphomevalonate kinase reaction is the delta, beta, gamma-bidentate complex. 31P NMR measurements and radioassay with [2-14C] phosphomevalonate were used to measure the equilibrium of the reaction catalyzed by phosphomevalonate kinase with ATP and phosphorothioate analogues of ATP as the phosphoryl group donor. The order as a phosphate donor as determined by both methods in the phosphomevalonate kinase reaction is ATP beta S greater than ATP alpha S greater than ATP greater than ATP gamma S. Except for ATP gamma S, the equilibrium is shifted in the direction of formation of ADP alpha S and ADP beta S relative to ADP formation. Thus, ATP beta S rather than ATP would be effective for the synthesis of diphosphomevalonate. The phosphomevalonate kinase reaction could also be used to synthesize mevalonate 5-(2-thiodiphosphate) using ATP gamma S as the phosphoryl group donor.",Nov 1985,"C S Lee, W J O'Sullivan"
+872,85LIE,,,,-,-,-,-,-,-,-,-
+873,85MAK/KIE,,10.1002/star.19850370706,,-,-,-,-,-,-,-,-
+874,85REK/SLO,,10.1016/0040-6031(85)85203-5,,-,-,-,-,-,-,-,-
+875,85SRI/FIS,3994979.0,10.1021/bi00324a012,,['eng'],24,3,618-22,Biochemistry,"The glutamate dehydrogenase catalyzed reduction of delta 1-pyrroline-2-carboxylic acid (PCA; an alpha-imino acid) with reduced nicotinamide adenine dinucleotide phosphate (NADPH) to give L-proline and NADP+ is employed as a model for the redox step of the corresponding enzyme-catalyzed reductive amination of alpha-ketoglutarate. We demonstrate the reversibility of the model reaction and measure its equilibrium constant. The pH profiles for the model reactions show that the active substrates are the N-protonated imino acid in one direction and the proline anion with a neutral amino group in the other. The V/K value for the imino acid reduction is enhanced by a group Z of pK = 8.6 in the enzyme-NADPH complex, while that for the proline reaction is unaffected by any such group in the enzyme-NADP+ complex. The following conclusions emerge from a comparison of the pH dependence of the rates for the model reactions with that for the oxidative deamination of L-glutamate [Rife, J. E., & Cleland, W. W. (1980) Biochemistry 19, 2328]. The N-protonated form of alpha-iminoglutarate and the conjugate base of glutamate are the active substrates. The redox step is not sensitive to the protonation state of the groups that catalyze the hydrolysis of bound alpha-iminoglutarate. The group Z, which facilitates the PCA reaction, plays no role in the binding of alpha-ketoglutarate. We propose a chemical mechanism for the glutamate reaction where an unprotonated enzyme group of pK = 5.2 in enzyme-NADPH catalyzes the conversion of the alpha-iminoglutarate to the carbinolamine.(ABSTRACT TRUNCATED AT 250 WORDS)",Jan 1985,"R Srinivasan, H F Fisher"
+876,85TEW/GOL,,10.1007/BF02824308,,-,-,-,-,-,-,-,-
+877,85TEW/GOL2,3931718.0,10.1016/0301-4622(85)80043-0,,['eng'],22,3,197-204,Biophysical chemistry,"The thermodynamics of the equilibria between aqueous ribose, ribulose, and arabinose were investigated using high-pressure liquid chromatography and microcalorimetry. The reactions were carried out in aqueous phosphate buffer over the pH range 6.8-7.4 and over the temperature range 313.15-343.75 K using solubilized glucose isomerase with either Mg(NO3)2 or MgSO4 as cofactors. The equilibrium constants (K) and the standard state Gibbs energy (delta G degrees) and enthalpy (delta H degrees) changes at 298.15 K for the three equilibria investigated were found to be: ribose(aq) = ribulose(aq) K = 0.317, delta G degrees = 2.85 +/- 0.14 kJ mol-1, delta H degrees = 11.0 +/- 1.5 kJ mol-1; ribose(aq) = arabinose(aq) K = 4.00, delta G degrees = -3.44 +/- 0.30 kJ mol-1, delta H degrees = -9.8 +/- 3.0 kJ mol-1; ribulose(aq) = arabinose(aq) K = 12.6, delta G degrees = -6.29 +/- 0.34 kJ mol-1, delta H degrees = -20.75 +/- 3.4 kJ mol-1. Information on rates of the above reactions was also obtained. The temperature dependencies of the equilibrium constants are conveniently expressed as R in K = -delta G degrees 298.15/298.15 + delta H degrees 298.15[(1/298.15)-(1/T)] where R is the gas constant (8.31441 J mol-1 K-1) and T the thermodynamic temperature.",Aug 1985,"Y B Tewari, R N Goldberg"
+878,85TEW/STE,17007786.0,10.1016/0301-4622(85)80041-7,,['eng'],22,3,181-5,Biophysical chemistry,"The thermodynamics of the conversion of aqueous xylose to xylulose has been investigated using high-pressure liquid chromatography (HPLC) and microcalorimetry. The reaction was carried out in aqueous phosphate buffer over the pH range 6.8-7.4 using solubilized glucose isomerase with MgSO(4) as a cofactor. The temperature range over which this reaction was investigated was 298.15-342.15 K. A combined analysis of both the HPLC and microcalorimetric data leads to the following results at 298.15 K for the conversion process: DeltaG degrees = 4389 +/- 31 J mol(-1), DeltaH degrees = 16090 +/- 670 J mol(-1), and DeltaC(p) degrees = 40 +/- 23 J mol(-1) K(-1). The temperature dependence of the equilibrium constant for the reaction is expressed as R ln K = -4389/298.15 +16090[(1/298.15)-(1/T)]+40[(298.15/T)-1 + ln(T/298.15)]. Comparisons are made with literature data.",Aug 1985,"Y B Tewari, D K Steckler, R N Goldberg"
+879,85VAN/SCH,2864395.0,10.1111/j.1471-4159.1985.tb07214.x,,['eng'],45,5,1471-4,Journal of neurochemistry,"The conversion of succinic semialdehyde into gamma-aminobutyric acid (GABA) by GABA-transaminase was measured in rat brain homogenate in the presence of different concentrations of the cosubstrate glutamate. The calculated kinetic parameters of succinic semialdehyde for GABA-transaminase were a limiting Km value of 168 microM and a limiting Vmax value of 38 mumol g-1 h-1. Combination with previously obtained data for the conversion of GABA into succinic semialdehyde revealed a kEq value of 0.04, indicating that equilibrium of GABA-transaminase is biased toward the formation of GABA. The increased formation of GABA in the presence of succinic semialdehyde was not due to an increased conversion of glutamate into GABA by glutamic acid decarboxylase. Therefore these results indicate that succinic semialdehyde can act as a precursor for GABA synthesis.",Nov 1985,"F J van Bemmelen, M J Schouten, D Fekkes, J Bruinvels"
+880,85WIE/HIN,3933423.0,10.1016/0003-9861(85)90228-0,,['eng'],242,2,440-6,Archives of biochemistry and biophysics,"The intrinsic enthalpy changes (corrected for hydration of D-glyceraldehyde 3-phosphate) for the reactions catalyzed by the alpha and beta 2 subunits of tryptophan synthase from Escherichia coli have been determined calorimetrically. Cleavage of indoleglycerol phosphate (alpha reaction) was found to be associated with a delta H value of 54.0 +/- 2.5 kJ mol-1, while condensation of indole with L-serine (beta reaction) involved -80.3 +/- 4.6 kJ mol-1'. By direct determination of the enthalpy concomitant with the overall synthesis of tryptophan from indoleglycerol phosphate and L-serine an enthalpy value of -13.4 +/- 5.6 kJ mol-1 was observed. In view of the uncertainties of the literature data used for calculation of the hydration contribution, the agreement between the directly measured delta H value of the overall reaction and the sum of the enthalpies of the alpha and beta reactions is fair. Deamination of L-serine, a side reaction catalyzed preferentially by the isolated beta 2 pyridoxal 5'-phosphate2 subunit, was shown to be associated with an enthalpy change of -7.3 +/- 0.4 kJ mol-1.",Nov 1985,"H Wiesinger, H J Hinz"
+881,86CAS/VEE,3826613.0,10.1016/0003-2697(86)90338-6,,['eng'],159,2,243-8,Analytical biochemistry,"A modification of the method of Kauffman et al. (F. C. Kauffman, J. G. Brown, J. V. Passonneau, and O. H. Lowry (1969) J. Biol. Chem. 244, 3647-3653) for the spectrophotometric determination of xylulose 5-phosphate, ribulose 5-phosphate, and combined ribose 5-phosphate and sedoheptulose 7-phosphate in tissue extract is presented. Using commercially available enzymes all three assays come to a clear endpoint with the assays described. Values for these metabolites in liver in three dietary states are reported; 48 h starved, ad libitum feeding of standard NIH rat ration, and meal feeding of a fat-free diet. Xylulose 5-phosphate values were 3.8 +/- 0.3, 8.6 +/- 0.3, and 66.3 +/- 8.3 nmol/g. Ribulose 5-phosphate values were 3.4 +/- 0.3, 5.8 +/- 0.2, and 37.1 +/- 5.3 nmol/g. Combined ribose 5-phosphate and sedoheptulose 7-phosphate were 29.3 +/- 0.3, 38.2 +/- 1.2, and 108.2 +/- 14.5 nmol/g. The ratio of measured tissue content of [xylulose 5-phosphate]/[ribulose 5-phosphate] was found to be 1.12 +/- 0.07 in starved animals, 1.48 +/- 0.04 in ad libitum fed animals and 1.78 +/- 0.03 in low-fat meal fed animals. These data are in good agreement with the range of equilibrium constants reported for this reaction, suggesting that the ribulose 5-phosphate 3-epimerase reaction (EC 5.1.3.1) is a near equilibrium reaction despite a more than 10-fold change in the tissue content of these metabolites.",Dec 1986,"J P Casazza, R L Veech"
+882,86CAS/VEE2,3079759.0,10.1016/S0021-9258(17)36148-3,,['eng'],261,2,690-8,The Journal of biological chemistry,"Equilibrium constants for reactions catalyzed by ribulose-5-phosphate 3-epimerase, [sigma xylulose-5-P]/[sigma ribulose-5-P] = 1.82, ribose-5-phosphate isomerase, [sigma Rib-5-P]/[sigma ribulose-5-P] = 1.20, transaldolase, [sigma erythrose-4-P] [sigma Fru-6-P]/[sigma sedoheptulose-7-P] [sigma glyceraldehyde 3-P] = 0.37, and transketolase, [sigma Fru-6-P] [sigma glyceraldehyde 3-P]/[sigma erythrose-4-P] [sigma xylulose-5-P] = 29.7 and [sigma Rib-5-P] [sigma xylulose-5-P]/[sigma sedoheptulose-7-P] [sigma glyceraldehyde 3-P] = 0.48, were redetermined under physiological conditions. The equilibrium constant for the combined glucose-6-P dehydrogenase and 6-phosphoglucono-gamma-lactonase reaction, [6-phosphogluconate3-] [NADPH] [H+]2/[Glc-6-P2-] [NADP+], was found to be at least 1 X 10(-9). Using these redetermined equilibrium constants, calculated values of pentose cycle intermediates, based on near equilibrium assumptions and the tissue content of Fru-6-P and glyceraldehyde 3-P, were found to be in good agreement with measured values for male Wistar rats injected with saline, 20 mumol/g pyruvate, 20 mumol/g gluconate, and 20 mumol/g ribose. Measured and calculated values for pentose cycle intermediates in saline injected animals were ribulose-5-P; 3.8 +/- 0.4 and 2.4 +/- 0.1 nmol/g; xylulose-5-P, 5.9 +/- 0.6 nmol/g and 4.3 +/- 0.2 nmol/g; sedoheptulose-7-P, 41.5 +/- 2.4 and 37.6 +/- 2.9 nmol/g; and combined sedopheptulose-7-P and Rib-5-P, 43.0 +/- 2.8 nmol/g and 40.5 +/- 3.0 nmol/g; liver content of erythrose-4-P was less than the detection limits of the assay, 2 nmol/g. Calculated erythrose-4-P was 0.23 +/- 0.01 nmol/g. Liver content of 6-phosphogluconate was 8.5 +/- 0.7 nmol/g. The free cytosolic [NADP+]/[NADPH] ratio calculated from the 6-phosphogluconate dehydrogenase redox couple, 0.0030 +/- 0.0002, was also in good agreement with that calculated from the malic enzyme redox couple, 0.0051 +/- 0.0007, and the isocitrate dehydrogenase redox couple, 0.0066 +/- 0.0008. These data indicate the interdependence of the liver content of glycolytic intermediates and pentose cycle intermediates in ad libitum fed rats.",Jan 1986,"J P Casazza, R L Veech"
+883,86DAL/REN,,10.1016/0003-2697(86)90642-1,,-,-,-,-,-,-,-,-
+884,86DEW/EMI,3741845.0,10.1021/bi00362a022,,['eng'],25,14,4132-40,Biochemistry,"The kinetic mechanism of AMP nucleosidase (EC 3.2.2.4; AMP + H2O----adenine + ribose 5-phosphate) from Azotobacter vinelandii is rapid-equilibrium random by initial rate studies of the forward and reverse reactions in the presence of MgATP, the allosteric activator. Inactivation-protection studies have established the binding of adenine to AMP nucleosidase in the absence of ribose 5-phosphate. Product inhibition by adenine suggests a dead-end complex of enzyme, AMP, and adenine. Methanol does not act as a nucleophile to replace H2O in the reaction, and products do not exchange into substrate during AMP hydrolysis. Thus, the reactive complex has the properties of concerted hydrolysis by an enzyme-directed water molecule rather than by formation of a covalent intermediate with ribose 5-phosphate. The Vmax in the forward reaction (AMP hydrolysis) is 300-fold greater than that in the reverse reaction. The Keq for AMP hydrolysis has been experimentally determined to be 170 M and is in reasonable agreement with Keq values of 77 and 36 M calculated from Haldane relationships. The equilibrium for enzyme-bound substrate and products strongly favors the enzyme-product ternary complex ([enzyme-adenine ribose 5-phosphate]/[enzyme-AMP] = 480). The temperature dependence of the kinetic constants gave Arrhenius plots with a distinct break between 20 and 25 degrees C. Above 25 degrees C, AMP binding demonstrates a strong entropic effect consistent with increased order in the Michaelis complex. Below 20 degrees C, binding is tighter and the entropic component is lost, indicating distinct enzyme conformations above and below 25 degrees C.(ABSTRACT TRUNCATED AT 250 WORDS)",Jul 1986,"W E DeWolf, F A Emig, V L Schramm"
+885,86GAJ/STE,3528161.0,10.1016/S0021-9258(18)67153-4,,['eng'],261,27,12733-7,The Journal of biological chemistry,"The enthalpy of hydrolysis of the enzyme-catalyzed (heavy meromyosin) conversion of adenosine 5'-triphosphate (ATP) to adenosine 5'-diphosphate (ADP) and inorganic phosphate has been investigated using heat-conduction microcalorimetry. Enthalpies of reaction were measured as a function of ionic strength (0.05-0.66 mol kg-1), pH (6.4-8.8), and temperature (25-37 degrees C) in Tris/HCl buffer. The measured enthalpies were adjusted for the effects of proton ionization and metal ion binding, protonation and interaction with the Tris buffer, and ionic strength effects to obtain a value of delta H0 = -20.5 +/- 0.4 kJ mol-1 at 25 degrees C for the process, ATP4-(aq) + H2O(l) = ADP3-(aq) + HPO2-4(aq) + H+(aq) where aq is aqueous and l is liquid. Heat measurements carried out at different temperatures lead to a value of delta C0p = -237 +/- 30 J mol-1 K-1 for the above process.",Sep 1986,"E Gajewski, D K Steckler, R N Goldberg"
+886,86GOL/GAJ,17007794.0,10.1016/0301-4622(86)85054-2,,['eng'],24,1,13-23,Biophysical chemistry,"The thermodynamics of the conversion of aqueous L-aspartic acid to fumaric acid and ammonia have been investigated using both heat conduction microcalorimetry and high-pressure liquid chromatography. The reaction was carried out in aqueous phosphate buffer over the pH range 7.25-7.43, the temperature range 13-43 degrees C, and at ionic strengths varying from 0.066 to 0.366 mol kg(-1). The following values have been found for the conversion of aqueous L-aspartateH- to fumarate2- and NH4+ at 25 degrees C and at zero ionic strength: K = (1.48 +/- 0.10) x 10(-3), DeltaG degrees = 16.15 +/- 0.16 kJ mol(-1), DeltaH degrees = 24.5 +/- 1.0 kJ mol(-1), and DeltaC(p) degrees = -147 +/- 100 J mol(-1) K(-1). Calculations have also been performed which give values of the apparent equilibrium constant for the conversion of L-aspartic acid to fumaric acid and ammonia as a function of temperature, pH and ionic strength.",Jun 1986,"R N Goldberg, E Gajewski, D K Steckler, Y B Tewari"
+887,86GRA/ELL,,10.1016/0167-4889(86)90050-9,,-,-,-,-,-,-,-,-
+888,86HUB/HUR,3083779.0,10.1016/0003-9861(86)90487-x,,['eng'],246,1,411-8,Archives of biochemistry and biophysics,"The reversion reactions of beta-galactosidase (Escherichia coli) produced beta-galactosyl-galactoses and beta-galactosyl-glucoses. About 10 beta-galactosyl-galactose and 10 beta-galactosyl-glucose gas-liquid chromatographic peaks were detected and it is thus very likely that every possible isomer of beta-galactosyl-galactose and beta-galactosyl-glucose was formed by the reversion reactions (taking into account both anomers for each isomer). The presence of lactose and allolactose among the beta-galactosyl-glucoses was confirmed with standards. An important finding relating to the role of allolactose as an inducer of the lac operon was that allolactose (beta-D-galactosyl-(1----6)-D-glucose) was the only disaccharide formed initially, and at equilibrium it was present in the largest amount (50%). Obviously the enzyme is specific in its ability to form allolactose, and allolactose is the most stable beta-galactosyl-glucose, both important inducer properties. The equilibrium constant (concentration of disaccharides divided by the concentration of reactants at equilibrium) of the reaction was about 9.5 mM-1. This is the first report of an equilibrium constant for the beta-galactosidase reaction. Of mechanistic significance is the fact that only three compounds were able to replace D-galactose as a reversion reactant. Two of these (L-arabinose and D-fucose) had alterations at carbon 6. The 6 position, therefore, is not essential for reactivity. The third compound was D-galactal. Any other sugars tested (even with very minor changes relative to D-galactose) did not react. Of special consequence is the 2 position. The results strongly suggest that there has to be either an equatorial hydroxyl at the 2 position of a sugar or a special reactivity (as with D-galactal) in order for the enzyme to catalyze the beta-galactosidase reaction.",Apr 1986,"R E Huber, K L Hurlburt"
+889,86KIM/LEE,,,,-,-,-,-,-,-,-,-
+890,86KON/POL,,10.1515/zna-1986-1203,,-,-,-,-,-,-,-,-
+891,86KUP/FER,,10.1016/0167-4838(86)90316-X,,-,-,-,-,-,-,-,-
+892,86MEI/GAD,,10.1007/BF00694264,,-,-,-,-,-,-,-,-
+893,86MEY/BRO,,10.1152/ajpcell.1986.250.2.C264,,-,-,-,-,-,-,-,-
+894,86NAK/KIM,3792308.0,10.1111/j.1432-1033.1986.tb10476.x,,['eng'],161,3,541-9,European journal of biochemistry,"We studied kinetics and the equilibrium relationship for the thermolysin-catalyzed synthesis of N-(benzyloxycarbonyl)-L-aspartyl-L-phenylalanine methyl ester (Z-Asp-PheOMe) from N-(benzyloxycarbonyl)-L-aspartic acid (Z-Asp) and L-phenylalanine methyl ester (PheOMe) in an aqueous-organic biphasic system. This is a model reaction giving a condensation product with dissociating groups. The kinetics for the synthesis of Z-Asp-PheOMe in aqueous solution saturated with ethyl acetate was expressed by a rate equation for the rapid-equilibrium random bireactant mechanism, and the reverse hydrolysis reaction was zero-order with respect to Z-Asp-PheOMe concentration. The courses of synthesis of Z-Asp-PheOMe in the biphasic system were well explained, by the rate equations obtained for the aqueous solution and by the partition of substrate and condensation product between the both phases. The rate of synthesis in the biphasic system was much lower than in aqueous solution due to the unfavorable partition of PheOMe in the aqueous phase. The equation for the equilibrium yield of Z-Asp-PheOMe in the biphasic system was derived assuming that only the non-ionized forms of the substrate and condensation product exist in the organic phase. It was found theoretically and experimentally that the yield of Z-Asp-PheOMe is maximum at the aqueous-phase pH of around 5, lower than for synthesis in aqueous solution. The effect of the organic solvent on the rate and equilibrium for the synthesis of Z-Asp-PheOMe could be explained by the variation in the partition coefficient. The effect of the partitioning of substrate on the aqueous-phase pH change was also shown.",Dec 1986,"K Nakanishi, Y Kimura, R Matsuno"
+895,86OLI/TOI,18555380.0,10.1002/bit.260280508,,['eng'],28,5,684-99,Biotechnology and bioengineering,"Both the forward and backward reactions of xylose isomerase (Sweetzyme Q) with xylose and glucose as substrates have been studied in terms of kinetics and thermodynamics. The relationship between the two reactions can thus be determined. Much attention has been given to the reaction with xylose as substrate. The optimal conditions of the xylose reaction in terms of pH, buffer, metal ions, substrate concentration, temperature, and ionic strength have been determined. These findings did not differ much from those reported for the glucose reaction. Equilibrium constants for the aldose to ketose conversion were more favorable in the case of glucose. The results obtained with continuous isomerization of xylose in columns packed with either Sweetzyme Q or Taka-Sweet were very similar to those obtained from batch isomerization processes. Particle size had a definite effect on reaction rate, which indicates that diffusion limitations do occur with the immobilized enzyme particles. Heat stability of Sweetzyme Q was good with t(1/2) of 118, 248, and 1200 h at 70, 55, and 40 degrees C, respectively. A novel method for the separation of xylose-xylulose mixtures with water as eluant on a specially prepared Dowex 1 x 8 column was developed. This technique has the capability of producing pure xylulose for industrial or research applications. A writ for a patent regarding this technique is at present prepared.",May 1986,"S P Olivier, P J du Toit"
+896,86POL/MEN,,,,-,-,-,-,-,-,-,-
+897,86PRU/TEN,,10.1016/0167-4838(86)90245-1,,-,-,-,-,-,-,-,-
+898,86RAG/CAR,3091600.0,10.1016/S0021-9258(18)67242-4,,['eng'],261,26,12324-9,The Journal of biological chemistry,"5'-Methylthioadenosine phosphorylase has been purified to homogeneity (30,000-fold) from human full-term placenta by a procedure involving covalent chromatography on organomercurial-agarose as the major step. The specific activity of the homogeneous enzyme is 10.2 mumol of 5'-methylthioadenosine cleaved per min per mg of protein, and the overall yield is about 20%. The enzyme has a molecular weight of 98,000, as determined by gel filtration on Sephacryl S-200 and Superose 6B, and is composed by three apparently identical subunits with a molecular weight of 32,500. The isoelectric point is 5.5, and the optimal pH ranges from 7.2 to 7.6. The resistance of the enzyme to thermal inactivation is increased remarkably by the addition of 5'-methylthioadenosine or phosphate. The homogeneous enzyme shows an absolute requirement for -SH-reducing agents and is specifically and rapidly inactivated by thiol-blocking compounds. The reaction catalyzed by the enzyme is fully reversible with a Keq of 1.39 X 10(-2) (in the direction of phosphorolysis) at 37 degrees C and pH 7.4. The Km values for 5'-methylthioadenosine, phosphate, adenine, and 5-methylthioribose 1-phosphate are 5, 320, 23, and 8 microM, respectively.",Sep 1986,"F Della Ragione, M Cartenì-Farina, V Gragnaniello, M I Schettino, V Zappia"
+899,86REK/SKY,,10.1016/0165-022X(86)90113-2,,-,-,-,-,-,-,-,-
+900,86ROH/ETT,3769932.0,10.1111/j.1432-1033.1986.tb09975.x,,['eng'],160,2,327-32,European journal of biochemistry,"Hog kidney aminoacylase (N-acylamino acid amidohydrolase; acylase I) is shown to catalyze the exchange of acetate oxygens with water at a significant rate only when alanine is present simultaneously. These studies, conducted using the 18O-isotope induced shift on 13C-NMR spectra, provide evidence in favor of a linear kinetic mechanism as opposed to a 'ping-pong' double-displacement mechanism. At pH values above neutrality, aminoacylase I also catalyzes the exchange of alanine oxygens with those of water. Ionic strength and pH effects on the kinetics of aminoacylase I are examined and the results are interpreted in terms of a model of the enzyme active site.",Oct 1986,"K H Röhm, R L Van Etten"
+901,86TEW/GOL,17007802.0,10.1016/0301-4622(86)85034-7,,['eng'],24,3,291-4,Biophysical chemistry,"The thermodynamics of the conversion of aqueous D-psicose to D-allose has been investigated using high-pressure liquid chromatography. The reaction was carried out in phosphate buffer at pH 7.4 over the temperature range 317.25-349.25 K. The following results are obtained for the conversion process at 298.15 K: DeltaG degrees = - 1.41 +/- 0.09 kJ mol(-1), DeltaH degrees = 7.42 +/- 1.7 kJ mol(-1), and DeltaC(p) degrees = 67 +/- 50 J mol(-1) K(-1). An approximate equilibrium constant of 0.30 is obtained at 333.15 K for the conversion of aqueous D-psicose to D-altrose. Available thermodynamic data for isomerization reactions involving aldohexoses and aldopentoses are summarized.",Aug 1986,"Y B Tewari, R N Goldberg"
+902,87ANT,,,,-,-,-,-,-,-,-,-
+903,87BED/TES,3429208.0,,,['eng'],36,4,243-55,The Italian journal of biochemistry,"A simple rate equation for alcohol dehydrogenase was obtained by assuming independent binding sites for ethanol and NAD+ and fully competitive inhibition by the products of the reaction, acetaldehyde and NADH. A random binding order was also assumed. The rate equation is described by six parameters: four association constants (two for the substrates and two for the products of the reaction), Vf for the forward direction, and the equilibrium constant of the reaction. The six parameters were determined at pH 7.4 by numerical analysis of progress curves of reactions started with different concentrations of ethanol and NAD+. The parameters for alcohol dehydrogenase partially purified from rat liver were: Km for ethanol = 0.746 mM, Km for NAD+ = 0.0563 mM, Km for acetaldehyde = 7.07 microM, Km for NADH = 4.77 microM and Keq = 2.36 X 10(-4). The computed values allowed a very good simulation of the experimental progress curves and little variation was observed in the kinetic parameters when the reactions were started in the presence of either NADH or acetaldehyde.", 1987,"S Bedino, G Testore, F Obert"
+904,87BUC/MIL,2883006.0,10.1111/j.1432-1033.1987.tb11164.x,,['eng'],164,3,565-9,European journal of biochemistry,"The equilibrium constants of the reactions catalysed by (S)-citramalate lyase and (R)-2-hydroxyglutarate dehydrogenase were determined using the purified enzymes from Clostridium tetanomorphum and Acidaminococcus fermentans, respectively. The former constant had to be determined at high ionic strength (I). Therefore it was corrected to I = 0.1 M by applying single-ion activity coefficients estimated from literature data. The result (Kapp = 4.31 +/- 0.07 M-1; direction of citramalate formation) agreed very well with the constant of the (2R,3S)-2,3-dimethylmalate lyase equilibrium when all optical isomers were taken into account. From these and other data values for the free energies of formation (delta Gzerof) of (2S,3S)-3-methylaspartate, mesaconate and (S)-citramalate were calculated. The constant of the (R)-2-hydroxyglutarate dehydrogenase equilibrium [Kapp = (1.47 +/- 0.12)10(-12) M, direction of 2-oxoglutarate formation, I = 0.1 M] was shown to lie between those for malate and lactate dehydrogenases as expected.",May 1987,"W Buckel, S L Miller"
+905,87FIE/JOH,3307916.0,10.1021/bi00387a052,,['eng'],26,13,4085-92,Biochemistry,"A kinetic scheme is presented for Escherichia coli dihydrofolate reductase that predicts steady-state kinetic parameters and full time course kinetics under a variety of substrate concentrations and pHs. This scheme was derived from measuring association and dissociation rate constants and pre-steady-state transients by using stopped-flow fluorescence and absorbance spectroscopy. The binding kinetics suggest that during steady-state turnover product dissociation follows a specific, preferred pathway in which tetrahydrofolate (H4F) dissociation occurs after NADPH replaces NADP+ in the ternary complex. This step, H4F dissociation from the E X NADPH X H4F ternary complex, is proposed to be the rate-limiting step for steady-state turnover at low pH because koff = VM. The rate constant for hydride transfer from NADPH to dihydrofolate (H2F), measured by pre-steady-state transients, has a deuterium isotope effect of 3 and is rapid, khyd = 950 s-1, essentially irreversible, Keq = 1700, and pH dependent, pKa = 6.5, reflecting ionization of a single group in the active site. This scheme accounts for the apparent pKa = 8.4 observed in the steady state as due to a change in the rate-determining step from product release at low pH to hydride transfer above pH 8.4. This kinetic scheme is a necessary background to analyze the effects of single amino acid substitutions on individual rate constants.",Jun 1987,"C A Fierke, K A Johnson, S J Benkovic"
+906,87HSU/WED,3322196.0,10.1016/0003-9861(87)90498-X,,['eng'],259,2,316-30,Archives of biochemistry and biophysics,"Equilibrium isotope exchange kinetics have been used to reinvestigate the kinetic mechanism of Escherichia coli aspartate transcarbamylase (aspartate carbamoyl-transferase) at pH 7.0, 30 degrees C. Keq = 5.9 (+/- 0.6) X 10(3), allowing variation of substrate concentrations above and below their Km values in all experiments, a condition not possible at pH 7.8 [F. C. Wedler and F. J. Gasser (1974) Arch. Biochem. Biophys. 163, 57-68]. The rate of the [14C]Asp in equilibrium N-carbamoyl L-aspartate (C-Asp) exchange reaction was five times faster than that of [32P]carbamyl phosphate (C-P) in equilibrium Pi, which argues strongly against the rapid equilibrium random mechanism previously proposed by E. Heyde, A. Nagabhushanam, and J. F. Morrison [Biochemistry 12, 4718-4726 (1973]. Substrate concentrations were varied either as reactant-product pairs (holding the other pair constant) or together simultaneously in constant ratio at equilibrium. The resulting kinetic saturation patterns were most consistent with a preferred order random kinetic mechanism, with C-P binding prior to Asp and with C-Asp being released before Pi. Weak inhibition effects at high substrate levels could be accounted for by multiple weak dead-end complexes or ionic strength effects. Computer-based simulations have led to a set of rate constants that fit the experimental data, are in agreement with rate constants measured previously by pre-steady-state methods, and predict the correct initial velocities in the forward and reverse directions. Simulations also show that rate constants consistent with any of the various alternative mechanisms do not provide good fit to the experimental data. A model for the kinetic mechanism is considered, in which the binding of Asp prior to C-P may restrict access of C-P to the active site, but C-P binding prior to Asp potentiates the enzyme for the allosteric (T-R) transition, centered entirely upon the Asp binding process.",Dec 1987,"Y Hsuanyu, F C Wedler"
+907,87KUC/MIZ,3327522.0,10.1021/bi00399a057,,['eng'],26,25,8410-7,Biochemistry,"The minimal kinetic scheme for DNA polymerization catalyzed by the Klenow fragment of DNA polymerase I (KF) from Escherichia coli has been determined with short DNA oligomers of defined sequence. A key feature of this scheme is a minimal two-step sequence that interconverts the ternary KF.DNAn.dNTP and KF.DNAn+1.PPi complexes. The rate is not limited by the actual polymerization but by a separate step, possibly important in ensuring fidelity [Mizrahi, V., Henrie, R. N., Marlier, J. F., Johnson, K. A., & Benkovic, S. J. (1985) Biochemistry 24, 4010-4018]. Evidence for this sequence is supplied by the observation of biphasic kinetics in single-turnover pyrophosphorolysis experiments (the microscopic reverse of polymerization). Data analysis then provides an estimate of the internal equilibrium constant. The dissociations of DNA, dNTP, and PPi from the various binary and ternary complexes were measured by partitioning (isotope-trapping) experiments. The rate constant for DNA dissociation from KF is sequence dependent and is rate limiting during nonprocessive DNA synthesis. The combination of single-turnover (both directions) and isotope-trapping experiments provides sufficient information to permit a quantitative evaluation of the kinetic scheme for specific DNA sequences.",Dec 1987,"R D Kuchta, V Mizrahi, P A Benkovic, K A Johnson, S J Benkovic"
+908,87MIL/EST,3597405.0,10.1016/S0021-9258(18)48039-8,,['eng'],262,19,9016-20,The Journal of biological chemistry,"2,5-Diketo-D-gluconate reductase, a novel enzyme that catalyzes the stereospecific NADPH-dependent reduction of 2,5-diketo-D-gluconate to 2-keto-L-gulonate, has been purified to homogeneity by sequential anion exchange, Cibacron blue F3GA affinity, and gel permeation chromatography from Corynebacterium sp. ATCC 31090. Molecular weight of the native form, determined by gel permeation chromatography, is 35,000 +/- 2,000. The subunit molecular weight, determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis is 34,000; thus, the enzyme is active as a monomer. A pI value of 4.4 is measured for the enzyme. Amino- and carboxyl-terminal sequences are consistent with that predicted by the DNA sequence of the reductase gene. At 25 degrees C, pH 6.4, the turnover number is 500 min-1, and the apparent Km values for 2,5-diketo-D-gluconate and NADPH are 26 mM and 10 microM, respectively. The enzyme is specific for NADPH, but the sugar binding site will also accept 5-keto-D-fructose and dihydroxyacetone as substrates. The enzyme is active over a broad pH range (pH 5-8) for the reduction of 2,5-diketo-D-gluconate; a sharp optimum at pH 9.2 is observed for the oxidation of 2-keto-L-gulonate. A Keq value of 5.6 X 10(-13) M indicates that reduction of substrate by NADPH is highly preferred. An activation energy of 12.3 kcal mol-1 is measured. Enzyme turnover is slow relative to dehydration of the gem-diol at C-5 of the substrate.",Jul 1987,"J V Miller, D A Estell, R A Lazarus"
+909,87MOS/FRE,3117791.0,10.1016/S0021-9258(18)48103-3,,['eng'],262,31,14859-62,The Journal of biological chemistry,"The interconversion of L-lysine and L-3,6-diamino-hexanoate (L-beta-lysine) catalyzed by lysine 2,3-aminomutase is known to be stimulated by added S-adenosylmethionine (Chirpich, T. P., Zappia, V., Costilow, R. N., and Barker, H. A. (1970) J. Biol. Chem. 245, 1778-1789). In this paper we show that enzyme activated by S-[2,8,5'-3H]adenosylmethionine catalyzes the conversion of L-lysine to the equilibrium mixture of L-lysine and L-beta-lysine with incorporation of high levels of tritium into both isomers. The tritium levels in the isomers reflect the equilibrium constant for their interconversion, 84% in the L-beta-lysine and 16% in L-lysine compared with Keq = 5.3 +/- 0.3 in the direction of the formation of L-beta-lysine at pH 7.7 and 30 degrees C. No significant tritium is incorporated into lysine from S-[2,8-3H]adenosylmethionine or S-adenosyl[methyl-3H] methionine under comparable conditions. Therefore, the tritium incorporated into lysine in the former reaction arises from the 5'-position of the 5'-deoxyadenosyl group in S-adenosylmethionine. These experiments implicate the 5'-deoxyadenosyl portion of S-adenosylmethionine in the hydrogen transfer mechanism of this reaction, perhaps in a role analogous to that played by the 5'-deoxyadenosyl moiety of deoxyadenosyl cobalamin in coenzyme B12-dependent rearrangements.",Nov 1987,"M Moss, P A Frey"
+910,87OWU/TRE,,10.1016/0040-6031(87)88028-0,,-,-,-,-,-,-,-,-
+911,87RAO/HAR,2958459.0,10.1016/S0021-9258(18)47906-9,,['eng'],262,29,14074-9,The Journal of biological chemistry,"The kinetic mechanism of phosphofructokinase has been determined at pH 8 for native enzyme and pH 6.8 for an enzyme desensitized to allosteric modulation by diethylpyrocarbonate modification. In both cases, the mechanism is predominantly steady state ordered with MgATP binding first in the direction of fructose 6-phosphate (F6P) phosphorylation and rapid equilibrium random in the direction of MgADP phosphorylation. This is a unique kinetic mechanism for a phosphofructokinase. Product inhibition by MgADP is competitive versus MgATP and noncompetitive versus F6P while fructose 1,6-bisphosphate (FBP) is competitive versus fructose 6-phosphate and uncompetitive versus MgATP. The uncompetitive pattern obtained versus F6P is indicative of a dead-end E.MgATP.FBP complex. Fructose 6-phosphate is noncompetitive versus either FBP or MgADP. Dead-end inhibition by arabinose 5-phosphate or 2,5-anhydro-D-mannitol 6-phosphate is uncompetitive versus MgATP corroborating the ordered addition of MgATP prior to F6P. In the direction of MgADP phosphorylation, inhibition by anhydromannitol 1,6-bisphosphate is noncompetitive versus MgADP, while Mg-adenosine 5'(beta, gamma-methylene)triphosphate is noncompetitive versus FBP. Anhydromannitol 6-phosphate is a slow substrate, while anhydroglucitol 6-phosphate is not. This suggests that the enzyme exhibits beta-anomeric specificity.",Oct 1987,"G S Rao, B G Harris, P F Cook"
+912,87REK/EGO,,10.1016/0040-6031(87)88272-2,,-,-,-,-,-,-,-,-
+913,87TAV/LEE,,10.1016/0167-4838(87)90136-1,,-,-,-,-,-,-,-,-
+914,87TEW/GAJ,,10.1021/j100288a028,,-,-,-,-,-,-,-,-
+915,87WOL/REI,,10.1016/S0006-3495(88)82934-5,,-,-,-,-,-,-,-,-
+916,88BED/HAD,3384815.0,10.1016/S0021-9258(19)81556-9,,['eng'],263,20,9582-8,The Journal of biological chemistry,"Chalcone isomerase from soybean has been purified 11,000-fold over the crude extract. The purification procedure features pseudo-affinity chromatography on an Amicon Matrex Orange A column with selective elution by a product of the enzymatic reaction. The purified enzyme is greater than 99.5% pure and possesses a specificity activity of 340 IU/mg, which is 520-fold greater than previously reported. The apparent molecular weight of the chalcone isomerase is 24,000 as determined from sodium dodecyl sulfate-polyacrylamide gels and from size exclusion chromatography under native conditions on Sephacryl S-200. The enzyme exists as a monomer that migrates on isoelectric focusing gels with a pI of 5.7. Amino acid analysis indicates that almost 50% of the residues are hydrophobic and yields a partial specific volume of 0.750 ml/g. Chalcone isomerase contains no carbohydrate moieties and has a blocked N terminus. The purified enzyme catalyzes the conversion of 2', 4',4-trihydroxychalcone (I) to (2S)-4',7-dihydroxyflavanone (II) at pH 7.6 with a second order rate constant, kcat/Km, of 1.1 X 10(9) M-1 min-1 and an apparent equilibrium constant, [II]/[I], of 7.6. The rate constant for the conversion of enzyme-bound substrate to the (2S)-flavanone, kcat = 11,000 min-1, exceeds the spontaneous conversion by 36 million-fold. The enzyme catalyzes the formation of (2S)-flavanone over 100,000-fold faster than to the (2R)-flavanone, indicating that the enzyme is highly stereoselective, yielding over 99.999% of the (2S)-flavanone.",Jul 1988,"R A Bednar, J R Hadcock"
+917,88BEL/BAE,2848810.0,10.1016/S0021-9258(18)37367-8,,['eng'],263,35,18897-903,The Journal of biological chemistry,"The membrane-associated phospholipid biosynthetic enzyme phosphatidylinositol kinase (ATP:phosphatidylinositol 4-phosphotransferase, EC 2.7.1.67) was purified 8,000-fold from Saccharomyces cerevisiae. The purification procedure included Triton X-100 solubilization of microsomal membranes, DE-52 chromatography, hydroxylapatite chromatography, octyl-Sepharose chromatography, and two consecutive Mono Q chromatographies. The procedure resulted in the isolation of a protein with a subunit molecular weight of 35,000 that was 96% of homogeneity as evidenced by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Phosphatidylinositol kinase activity was associated with the purified Mr 35,000 subunit. Maximum phosphatidylinositol kinase activity was dependent on magnesium ions and Triton X-100 at pH 8. The true Km values for phosphatidylinositol and MgATP were 70 microM and 0.3 mM, and the true Vmax was 4,750 nmol/min/mg. The turnover number for the enzyme was 166 min-1. Results of kinetic and isotopic exchange reactions indicated that phosphatidylinositol kinase catalyzed a sequential Bi Bi reaction mechanism. The enzyme bound to phosphatidylinositol prior to ATP and phosphatidylinositol 4-phosphate was the first product released in the reaction. The equilibrium constant for the reaction indicated that the reverse reaction was favored in vitro. The activation energy for the reaction was 31.5 kcal/mol, and the enzyme was thermally labile above 30 degrees C. Phosphatidylinositol kinase activity was inhibited by calcium ions and thioreactive agents. Various nucleotides including adenosine and S-adenosylhomocysteine did not affect phosphatidylinositol kinase activity.",Dec 1988,"C J Belunis, M Bae-Lee, M J Kelley, G M Carman"
+918,88GAU,2844813.0,10.1016/S0021-9258(19)37602-1,,['eng'],263,30,15400-6,The Journal of biological chemistry,"Phosphoglycerate mutase (GPM) functions reversibly in the glycolytic pathway. Mutations altering the reversibility of GPM have been obtained in the yeast, Saccharomyces cerevisiae. While wild-type cells grow on glycolytic (glucose) or gluconeogenic (ethanol) substrates, cells with altered GPMs fall into three categories based on their phenotypes 1) glucose- ethanol-, 2) glucose+ ethanol-, and 3) glucose- ethanol+. Cells with the first two phenotypes possessed GPMs that functioned irreversibly in the glycolytic direction. Cells that were glucose- ethanol+ possessed an enzyme that functioned reversibly. All of the altered GPMs had maximal velocities that were less than 3% of the wild-type level. The properties of the altered GPMs studied here provide a rationale for the occurrence in the glycolytic pathway of several glycolytic enzymes such as GPM, which function at high velocities in relation to the much smaller metabolic flux that they support. The altered GPMs were purified and estimates of their kinetic constants obtained. Free energy profiles were drawn for catalysis by the wild type and a mutant GPM that functioned irreversibly. The mutant enzyme was very inefficient. It was shown that an enzyme that functions irreversibly at a reaction with a Keq value close to 1 would necessarily be inefficient while it could evolve to be efficient when catalyzing a reaction that has a Keq value much greater than 1. In the glycolytic path this could be the reason for the characteristic presence of enzymes that function irreversibly at reactions with large Keq values.",Oct 1988,N Gautam
+919,88GUI/SNE,3076441.0,,,['eng'],1,2,187-92,"BioFactors (Oxford, England)","Pyridoxine dehydrogenase (1.1.1.65) (pyridoxal reductase), purified to homogeneity from baker's yeast, is a monomer of Mr approximately 33,000. It catalyzes the reversible oxidation of pyridoxine by NADP to yield pyridoxal and NADPH; equilibrium lies far in the direction of pyridoxine formation (Keq approximately 1.4 X 10(11) l/mol at 25 degrees C). Reduction of pyridoxal occurs most rapidly at pH 6.0-7.0; oxidation of pyridoxine is optimal at pH 8.6. NAD and NADH do not replace NADP and NADPH as substrates; pyridoxine, pyridoxal and pyridoxal 5'-phosphate are the only naturally occurring cosubstrates found. Several other aromatic aldehydes also are reduced, but substrate specificity and other properties of the enzyme distinguish it clearly from other alcohol dehydrogenases or aldehyde reductases. Between pH 6.3 and 7.1 (the intracellular pH of yeast), V/Km with pyridoxal and NADPH as substrates is greater than 600 times that observed with pyridoxine and NADPH as substrates is greater than 600 times that observed with pyridoxine and NADP as substrates. These and other considerations strongly indicate that the dehydrogenase functions in vivo to reduce pyridoxal to pyridoxine, which is the preferred substrate for pyridoxal (pyridoxine) kinase in yeast.",Jul 1988,"B M Guirard, E E Snell"
+920,88LIM/RAI,3365378.0,10.1021/bi00404a013,,['eng'],27,4,1158-67,Biochemistry,"The rates of the forward and reverse reactions of triosephosphate isomerase catalyzed by the wild-type and by a sluggish mutant enzyme have been studied in the absence and the presence of several viscosogenic agents. For the mutant enzyme, the kcat for which is some 10(3) times less than that for the wild-type enzyme, the value of kcat/Km with glyceraldehyde phosphate as substrate is almost unaffected by the presence of sucrose or glycerol, even though the concentration of the aldehyde form of the substrate is smaller because of hemiacetal formation. [The nature and relative amounts of the various forms of triose phosphate present in solution (free carbonyl forms, hydrates, dimers, hemiacetal adducts) have been evaluated by 31P NMR and are presented in the Appendix.] The viscosogenic agents cause the substrate to bind more tightly to the enzyme, roughly compensating for the lower substrate concentration. With dihydroxyacetone phosphate as substrate, the values of kcat/Km for the mutant enzyme increase with the addition of viscosogenic agent, consistent with the tighter binding of substrate without (in this case) any concomitant loss due to hemiketal formation. These results for the mutant enzyme (known to be limited in rate by an enolization step in the catalytic mechanism) can be used to interpret the behavior of the wild-type enzyme. Plots of the relative values of kcat/Km for catalysis by the wild-type enzyme (normalized with the corresponding data for the mutant enzyme) against the relative viscosity have slopes close to unity, as predicted by the Stokes-Einstein equation for a cleanly diffusive process. In the presence of polymeric viscosogenic additives such as poly(ethylene glycol), polyacrylamide, or ficoll, no effect on kcat/Km is seen for the wild-type enzyme, consistent with the expectation that molecular diffusion rates are unaffected by the macroviscosity and are only slowed by the presence of smaller agents that raise the microviscosity. These results show that the reaction catalyzed by the wild-type triosephosphate isomerase is limited by the rate at which glyceraldehyde phosphate encounters, or departs from, the active site.",Feb 1988,"S C Blacklow, R T Raines, W A Lim, P D Zamore, J R Knowles"
+921,88MAC/FEW,3291854.0,10.1042/bj2500743,,['eng'],250,3,743-51,The Biochemical journal,"A quick, reliable, purification procedure was developed for purifying both benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II from a single batch of Acinetobacter calcoaceticus N.C.I.B. 8250. The procedure involved disruption of the bacteria in the French pressure cell and preparation of a high-speed supernatant, followed by chromatography on DEAE-Sephacel, affinity chromatography on Blue Sepharose CL-6B and Matrex Gel Red A, and finally gel filtration through a Superose 12 fast-protein-liquid-chromatography column. The enzymes co-purified as far as the Blue Sepharose CL-6B step were separated on the Matrex Gel Red A column. The final preparations of benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II gave single bands on electrophoresis under non-denaturing conditions or on SDS/polyacrylamide-gel electrophoresis. The enzymes are tetramers, as judged by comparison of their subunit (benzyl alcohol dehydrogenase, 39,700; benzaldehyde dehydrogenase II, 55,000) and native (benzyl alcohol dehydrogenase, 155,000; benzaldehyde dehydrogenase II, 222,500) Mr values, estimated by SDS/polyacrylamide-gel electrophoresis and gel filtration respectively. The optimum pH values for the oxidation reactions were 9.2 for benzyl alcohol dehydrogenase and 9.5 for benzaldehyde dehydrogenase II. The pH optimum for the reduction reaction for benzyl alcohol dehydrogenase was 8.9. The equilibrium constant for oxidation of benzyl alcohol to benzaldehyde by benzyl alcohol dehydrogenase was determined to be 3.08 x 10(-11) M; the ready reversibility of the reaction catalysed by benzyl alcohol dehydrogenase necessitated the development of an assay procedure in which hydrazine was used to trap the benzaldehyde formed by the NAD+-dependent oxidation of benzyl alcohol. The oxidation reaction catalysed by benzaldehyde dehydrogenase II was essentially irreversible. The maximum velocities for the oxidation reactions catalysed by benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II were 231 and 76 mumol/min per mg of protein respectively; the maximum velocity of the reduction reaction of benzyl alcohol dehydrogenase was 366 mumol/min per mg of protein. The pI values were 5.0 for benzyl alcohol dehydrogenase and 4.6 for benzaldehyde dehydrogenase II. Neither enzyme activity was affected when assayed in the presence of a range of salts. Absorption spectra of the two enzymes showed no evidence that they contain any cofactors such as cytochrome, flavin, or pyrroloquinoline quinone. The kinetic coefficients of the purified enzymes with benzyl alcohol, benzaldehyde, NAD+ and NADH are also presented.",Mar 1988,"R W MacKintosh, C A Fewson"
+922,88TEW/GOL,2839246.0,10.1016/0301-4622(88)85045-2,,['eng'],29,3,245-52,Biophysical chemistry,"The thermodynamics of the enzymatic conversion (penicillin acylase) of aqueous penicillin G to phenylacetic acid and 6-aminopenicillanic acid have been studied using both high-pressure liquid-chromatography and microcalorimetry. The reaction was carried out in aqueous phosphate buffer over the pH range 6.0-7.6, at ionic strengths from 0.10 to 0.40 mol kg-1, and at temperatures from 292 to 322 K. The data have been analyzed using a chemical equilibrium model with an extended Debye-Hückel expression for the activity coefficients. For the reference reaction, penicillin G- (aq) + H2O(l) = phenylacetic acid-(aq) + 6-aminopenicillanic acid-(aq) + H+ (aq), the following parameters have been obtained: K = (7.35 +/- 1.5) X 10(-8) mol kg-1, delta G0 = 40.7 +/- 0.5 kJ mol-1, delta H0 = 29.7 +/- 0.6 kJ mol-1, and delta C0p = -240 +/- 50 J mol-1 K-1 at 298.15 K and at the thermochemical standard state. The extent of reaction for the overall conversion is highly dependent upon the pH.",Apr 1988,"Y B Tewari, R N Goldberg"
+923,88TEW/STE,3346215.0,10.1016/S0021-9258(18)68976-8,,['eng'],263,8,3664-9,The Journal of biological chemistry,"Thermodynamics of isomerization reactions involving sugar phosphates have been studied using heat-conduction microcalorimetry. For the process glucose 6-phosphate2-(aqueous) = fructose 6-phosphate2- (aqueous), K = 0.285 +/- 0.004, delta Go = 3.11 +/- 0.04 kJ.mol-1, delta Ho = 11.7 +/- 0.2 kJ.mol-1, and delta Cop = 44 +/- 11 J.mol-1.K-1 at 298.15 K. For the process mannose 6-phosphate2- (aqueous) = fructose 6-phosphate2- (aqueous), K = 0.99 +/- 0.05, delta Go = 0.025 +/- 0.13 kJ.mol-1, delta Ho = 8.46 +/- 0.2 kJ.mol-1, and delta Cop = 38 +/- 25 J.mol-1.K-1 at 298.15 K. The standard state is the hypothetical ideal solution of unit molality. An approximate result (-14 +/- 5 kJ.mol-1) was obtained for the enthalpy of isomerization of ribulose 5-phosphate (aqueous) to ribose 5-phosphate (aqueous). The data from the literature on isomerization reactions involving sugar phosphates have been summarized, adjusted to a common reference state, and examined for trends and relationships to each other and to other thermodynamic measurements. Estimates are made for thermochemical parameters to predict the state of equilibrium of the several isomerizations considered herein.",Mar 1988,"Y B Tewari, D K Steckler, R N Goldberg"
+924,88TEW/STE2,3346216.0,10.1016/S0021-9258(18)68977-X,,['eng'],263,8,3670-5,The Journal of biological chemistry,"Thermodynamics of the enzyme-catalyzed (alkaline phosphatase, EC 3.1.3.1) hydrolysis of glucose 6-phosphate, mannose 6-phosphate, fructose 6-phosphate, ribose 5-phosphate, and ribulose 5-phosphate have been investigated using microcalorimetry and, for the hydrolysis of fructose 6-phosphate, chemical equilibrium measurements. Results of these measurements for the processes sugar phosphate2- (aqueous) + H2O (liquid) = sugar (aqueous) + HPO2++-(4) (aqueous) at 25 degrees C follow: delta Ho = 0.91 +/- 0.35 kJ.mol-1 and delta Cop = -48 +/- 18 J.mol-1.K-1 for glucose 6-phosphate; delta Ho = 1.40 +/- 0.31 kJ.mol-1 and delta Cop = -46 +/- 11 J.mol-1.dK-1 for mannose 6-phosphate; delta Go = -13.70 +/- 0.28 kJ.mol-1, delta Ho = -7.61 +/- 0.68 kJ.mol-1, and delta Cop = -28 +/- 42 J.mol-1.K-1 for fructose 6-phosphate; delta Ho = -5.69 +/- 0.52 kJ.mol-1 and delta Cop = -63 +/- 37 J.mol-1.K-1 for ribose 5-phosphate; and delta Ho = -12.43 +/- 0.45 kJ.mol-1 and delta Cop = -84 +/- 30 J.mol-1.K-1 for the hydrolysis of ribulose 5-phosphate. The standard state is the hypothetical ideal solution of unit molality. Estimates are made for the equilibrium constants for the hydrolysis of ribose and ribulose 5-phosphates. The effects of pH, magnesium ion concentration, and ionic strength on the thermodynamics of these reactions are considered.",Mar 1988,"Y B Tewari, D K Steckler, R N Goldberg, W L Gitomer"
+925,89AIR,,10.3891/acta.chem.scand.43-0386,,-,-,-,-,-,-,-,-
+926,89BER/MUD,,10.1016/0165-022X(89)90073-0,,-,-,-,-,-,-,-,-
+927,89ELD/DEG,,10.1002/mrm.1910110111,,-,-,-,-,-,-,-,-
+928,89ELL,2543728.0,10.1242/jeb.143.1.177,,['eng'],143,-,177-94,The Journal of experimental biology,"In vertebrate tissues, the only phosphagen is phosphocreatine (PC), and the corresponding phosphotransferase is creatine phosphokinase (CPK). Among invertebrates, a variety of phosphotransferase reactions are found in addition to CPK, including arginine phosphokinase (APK), glycocyamine phosphokinase (GPK), taurocyamine phosphokinase (TPK) and lombricine phosphokinase (LPK). Although there is some uncertainty about the exact value, the apparent equilibrium constant for the CPK reaction (K'cpk = [creatine][ATP]/[PC][ADP]), under physiological conditions similar to those of vertebrate muscle, ranges from 100 to 160. The corresponding K' value for the APK reaction is somewhat controversial, and K' values for the GPK. TPK and LPK reactions are not known. In this study, conventional and 31P-NMR methods were used to evaluate the equilibrium constants for the APK, GPK, TPK and LPK reactions relative to that of CPK. The corresponding K' values for the APK, GPK, TPK and LPK reactions, expressed as a percentage of K'cpk, are 13, 29, 29 and 32%, respectively. The exclusively invertebrate phosphagens exist as a cohort of thermodynamically more stable compounds. Thus, PC constitutes a thermodynamic (and functional) improvement, in that the CPK reaction is able to buffer ATP at much higher ATP/ADP ratios than are other phosphagens. However, possession of a phosphagen system with a lower K' value may be advantageous under certain specific physiological conditions such as intracellular acidosis.",May 1989,W R Ellington
+929,89GOL/TEW,2498341.0,10.1016/S0021-9258(18)81743-4,,['eng'],264,17,9897-900,The Journal of biological chemistry,"The thermodynamics of the hydrolysis of lactose to glucose and galactose have been investigated using both high pressure liquid chromatography and heat-conduction microcalorimetry. The reaction was carried out over the temperature range 282-316 K and in 0.1 M sodium acetate buffer at a pH of 5.65 using the enzyme beta-galactosidase to catalyze the reaction. For the process lactose(aq) + H2O(liq) = glucose(aq) + galactose(aq), delta G0 = -8.72 +/- 0.20 kJ.mol-1, K0 = 34 +/- 3, delta H0 = 0.44 +/- 0.11 kJ.mol-1, delta S0 = 30.7 +/- 0.8 J.mol-1.K-1, and delta Cop = 9 +/- 20 J.mol-1.K-1 at 298.15 K. The standard state is the hypothetical ideal solution of unit molality. Thermochemical cycle calculations using enthalpies of combustion and solution, entropies, solubilities, activity coefficients, and apparent molar heat capacities have also been performed. These calculations indicate large discrepancies which are attributable primarily to errors in literature data on the enthalpies of combustion and/or third law entropies of the crystalline forms of the substrates.",Jun 1989,"R N Goldberg, Y B Tewari"
+930,89GOL/TEW2,2722882.0,10.1016/S0021-9258(18)81744-6,,['eng'],264,17,9901-4,The Journal of biological chemistry,"A thermodynamic investigation of the hydrolysis of sucrose to fructose and glucose has been performed using microcalorimetry and high-pressure liquid chromatography. The calorimetric measurements were carried out over the temperature range 298-316 K and in sodium acetate buffer (0.1 M, pH 5.65). Enthalpy and heat capacity changes were obtained for the hydrolysis of aqueous sucrose (process A): sucrose(aq) + H2O(liq) = glucose(aq) + fructose (aq). The determination of the equilibrium constant required the use of a thermochemical cycle calculation involving the following processes: (B) glucose 1-phosphate2-(aq) = glucose 6-phosphate2-(aq); (C) sucrose(aq) + HPO4(2-)(aq) = glucose 1-phosphate2-(aq) + fructose(aq); and (D) glucose 6-phosphate2-(aq) + H2O(liq) = glucose(aq) + HPO4(2-)(aq). The equilibrium constants determined at 298.15 K for processes B and C are 17.1 +/- 1.0 and 32.4 +/- 3.0, respectively. Equilibrium data for process D was obtained from the literature, and in conjunction with the data for processes B and C, used to calculate a value of the equilibrium constant for the hydrolysis of aqueous sucrose. Thus, for process A, delta G0 = -26.53 +/- 0.30 kJ mol-1, K0 = (4.44 +/- 0.54) x 10(4), delta H0 = -14.93 +/- 0.16 kJ mol-1, delta So = 38.9 +/- 1.2 J mol-1 K-1, and delta CoP = 57 +/- 14 J mol-1 K-1 at 298.15 K. Additional thermochemical cycles that bear upon the accuracy of these results are examined.",Jun 1989,"R N Goldberg, Y B Tewari, J C Ahluwalia"
+931,89HAG/ROS,2537492.0,10.1073/pnas.86.4.1224,,['eng'],86,4,1224-8,Proceedings of the National Academy of Sciences of the United States of America,"The sensory dark current of vertebrate retinal rods is believed to be controlled by light activation of a chain of coupled biochemical cycles that finally regulate the cationic conductance of the plasma membrane by hydrolytically reducing the level of cGMP in rod outer segment cytoplasm. The scheme has been tested by measuring heat production by live frog retinas when stimulated with sequences of light flashes of progressively increasing energy. Using pyroelectric poly(vinylidene 1,1-difluoride) detectors that simultaneously measure transretinal voltage and retinal temperature change, four heat effects assignable to known biochemical cycles in rods have been found. As the dark current shuts down after a flash causing 180-1800 rhodopsin photoisomerizations per rod, a heat burst, q1, raises the retinal temperature 1-2 microK. q1 is closely regulated in size and slightly precedes dark current shutdown. Isobutylmethylxanthine slows and enlarges q1, delaying the dark-current response. Increasing cytoplasmic Ca2+ stops the dark current without affecting q1. Although rod heat production is consistent with splitting of 1-3 microM of free cytoplasmic cGMP during transduction, the kinetics of the two processes do not match the predictions of current cGMP control models.",Feb 1989,"W A Hagins, P D Ross, R L Tate, S Yoshikami"
+932,89IMA,,10.1093/oxfordjournals.jbchem.a122954,,-,-,-,-,-,-,-,-
+933,89JEE/SHI,,,,-,-,-,-,-,-,-,-
+934,89JOH/HED,,10.1016/0141-0229(89)90018-5,,-,-,-,-,-,-,-,-
+935,89JUN/JUN,2663076.0,10.1016/0005-2760(89)90232-4,,['eng'],1003,3,270-6,Biochimica et biophysica acta,"Carnitine dehydratase from Escherichia coli 044 K74 is an inducible enzyme detectable in cells grown anaerobically in the presence of L(-)-carnitine or crotonobetaine. It has been purified 500-fold to electrophoretic homogeneity by chromatography on phenyl-Sepharose, hydroxyapatite, DEAE-Sepharose, second phenyl-Sepharose and finally gel filtration on a Sephadex G-100 column. During the purification procedure a low-molecular-weight effector essential for enzyme activity was separated from the enzyme. The addition of this still unknown effector caused reactivation of the apoenzyme. The relative molecular mass of the apoenzyme has been estimated to be 85,000. It seems to be composed of two identical subunits with a relative molecular mass of 45,000. The purified and reactivated enzyme has been further characterized with respect to pH and temperature optimum (7.8 and 37-42 degrees C), equilibrium constant (Keq = 1.5 +/- 0.2) and substrate specifity. The enzyme is inhibited by thiol reagents. The Km value for crotonobetaine is 1.2.10(-2) M. gamma-Butyrobetaine, D(+)-carnitine and choline are competitive inhibitors of crotonobetaine hydration.",Jun 1989,"H Jung, K Jung, H P Kleber"
+936,89LEH/SIN,2494984.0,10.1042/bj2570355,,['eng'],257,2,355-9,The Biochemical journal,"1. alpha-Deuterium kinetic isotope effects on the phosphorolysis of inosine catalysed by Escherichia coli purine nucleoside phosphorylase were measured by the equilibrium-perturbation technique, by using the change in absorbance at 250 nm (approx. 20%). 2. Values of 2H(V/K) of 1.13(9) at pH 5.0, 1.10(5) at pH 6.1, 1.09(4) at pH 7.3, 1.08 at pH 8.4 and 1.16(4) at pH 9.4 were obtained. 3. These are compared with literature alpha-deuterium kinetic isotope effects for this and related reactions. 4. The equilibrium constant, defined as [inosine].[H2PO4-]/[hypoxanthine] [alpha-Rib f OPO3H-], is 46 at 25 degrees C. 5. N-3-beta-D-Ribofuranosylhypoxanthine, an impurity in chemically synthesized inosine, is a substrate.",Jan 1989,"P K Lehikoinen, M L Sinnott, T A Krenitsky"
+937,89LOP/COH,,10.1016/0167-4838(89)90291-4,,-,-,-,-,-,-,-,-
+938,89REK/SIK,,,,-,-,-,-,-,-,-,-
+939,89RIZ/HAR,,10.1016/0922-338X(89)90081-0,,-,-,-,-,-,-,-,-
+940,89ROM/DEM,2722769.0,10.1016/S0021-9258(18)83123-4,,['eng'],264,14,7869-73,The Journal of biological chemistry,"The observed equilibrium constants for hydrolysis (Kobs) of a phosphoester and a phosphoanhydride bond were measured under a variety of conditions likely to alter the interactions of reactants and products with water. These included increasing the pH of the medium from 5.0 to 10.0, increasing the MgCl2 concentration form 0 to 200 mM, and decreasing the water activity of the medium by adding either dimethyl sulfoxide (50%, v/v) or polyethylene glycol 6,000-8,000 (50%, w/v). The Kobs for phosphoesters such as phosphoserine, glucose phosphate, glycerol phosphate, and ethylene glycol phosphate varied little over this wide range of conditions, the extreme values of Kobs being 12 and 200 M. In contrast, the Kobs for the phosphoanhydride bond of pyrophosphate varied from a value greater than 20,000 to 0.1 M. In totally aqueous media at a pH between 7.0 and 8.0 and in the presence of 0.5-1.0 mM MgCl2, the energy of hydrolysis of pyrophosphate was 1.2-4.0 kcal/mol greater than that of phosphoserine. However, when the water activity was decreased by adding polyethylene glycol to the medium within the same pH and MgCl2 concentration range, the energy of hydrolysis of phosphoserine became 2.0-2.5 kcal/mol greater than that of pyrophosphate. The results suggest that for phosphoesters, the solvation energies of reactants and products, unlike the case of phosphoanhydride bonds, are not the major factors in determining the energy of hydrolysis.",May 1989,"P J Romero, L de Meis"
+941,89SAN/SIN,,10.1007/BF02703521,,-,-,-,-,-,-,-,-
+942,89SCH/GIF,2789134.0,10.1111/j.1432-1033.1989.tb14984.x,,['eng'],184,1,15-9,European journal of biochemistry,"A polyol dehydrogenase was detected in cell extracts of the facultative phototrophic bacterium Rhodobacter sphaeroides strain Si 4 grown on D-glucitol (sorbitol) as the sole carbon source. The enzyme was purified 150-fold to apparent homogeneity by steps involving fractionated (NH4)2SO4 precipitation, chromatography on Q-Sepharose and phenyl-Sepharose, and FPLC on Superose 12. The relative molecular mass (Mr) of the native polyol dehydrogenase was 47,200 as calculated from its Stokes' radius (rs = 2.76 nm) and sedimentation coefficient (s20, w = 4.15 S). SDS/PAGE resulted in one single band representing a polypeptide with a Mr of 52,200, indicating that the native protein is a monomer. The isoelectric point of the polyol dehydrogenase was determined to be pH 4.3. The enzyme was specific for NAD+ and oxidized both D-glucitol and D-mannitol to D-fructose, as well as D-arabinitol to D-ribulose. The pH optimum of substrate oxidation was pH 9.0 in 0.1 M Tris/HCl and that of substrate reduction was pH 6.5 in 0.1 M potassium phosphate. The reactions exhibited normal Michaelis-Menten kinetics allowing the estimation of KM values for NAD+ (0.18 mM) in the presence of D-glucitol, and for D-glucitol (31.8 mM), D-mannitol (0.29 mM) and D-arabinitol (1.8 mM), respectively. The KM value for D-fructose was 16.3 mM and that for NADH 0.02 mM. The equilibrium constants determined for the conversion of D-mannitol, D-glucitol and D-arabinitol were 4.5 nM, 0.58 nM and 80 pM, respectively. Based on the catalytic preference of the polyol dehydrogenase for D-mannitol, an enzymatic assay for D-mannitol was elaborated.",Sep 1989,"K H Schneider, F Giffhorn"
+943,89TEW/GOL,2492994.0,10.1016/S0021-9258(19)84947-5,,['eng'],264,7,3966-71,The Journal of biological chemistry,"The thermodynamics of the enzymatic hydrolysis of cellobiose, gentiobiose, isomaltose, and maltose have been studied using both high pressure liquid chromatography and microcalorimetry. The hydrolysis reactions were carried out in aqueous sodium acetate buffer at a pH of 5.65 and over the temperature range of 286 to 316 K using the enzymes beta-glucosidase, isomaltase, and maltase. The thermodynamic parameters obtained for the hydrolysis reactions, disaccharide(aq) + H2O(liq) = 2 glucose(aq), at 298.15 K are: K greater than or equal to 155, delta G0 less than or equal to -12.5 kJ mol-1, and delta H0 = -2.43 +/- 0.31 kJ mol-1 for cellobiose; K = 17.9 +/- 0.7, delta G0 = -7.15 +/- 0.10 kJ mol-1 and delta H0 = 2.26 +/- 0.48 kJ mol-1 for gentiobiose; K = 17.25 +/- 0.7, delta G0 = -7.06 +/- 0.10 kJ mol-1, and delta H0 = 5.86 +/- 0.54 kJ mol-1 for isomaltose; and K greater than or equal to 513, delta G0 less than or equal to -15.5 kJ mol-1, and delta H0 = -4.02 +/- 0.15 kJ mol-1 for maltose. The standard state is the hypothetical ideal solution of unit molality. Due to enzymatic inhibition by glucose, it was not possible to obtain reliable values for the equilibrium constants for the hydrolysis of either cellobiose or maltose. The entropy changes for the hydrolysis reactions are in the range 32 to 43 J mol-1 K-1; the heat capacity changes are approximately equal to zero J mol-1 K-1. Additional pathways for calculating thermodynamic parameters for these hydrolysis reactions are discussed.",Mar 1989,"Y B Tewari, R N Goldberg"
+944,90BHA/VIN,2271660.0,10.1021/bi00498a009,,['eng'],29,46,10480-7,Biochemistry,"The chemical mechanism of the phosphoribosyltransferases (PRTases), although largely unknown, may proceed either via a concerted direct-transfer mechanism or with a two-step mechanism involving a carboxonium-like intermediate. To study this question, we have cloned the Salmonella typhimurium pyrE gene, coding for the enzyme orotate phosphoribosyltransferase (EC 2.2.4.10, OPRTase), and developed a bacterial strain that overproduces the enzyme, which we have purified to homogeneity. Initial velocity and product inhibition studies indicated that S. typhimurium OPRTase follows a random sequential kinetic mechanism. This result was further confirmed by equilibrium isotope exchange studies on two substrate-product pairs, PRPP-PPi and OMP-orotate. In addition, the rates of the individual equilibrium isotope exchanges allowed us to conclude that PPi release and PRPP release were the rate-determining steps in the forward and reverse reactions, respectively. Although partial reactions between the two substrate-product pairs, PRPP-PPi and OMP-orotate, were observed, further studies revealed that these exchanges were a result of contaminations. Our results are significant in that S. typhimurium OPRTase, like most PRTases but in contrast to its yeast homologue, follows sequential kinetics. The artifactual partial isotope exchanges found in this work may have implications for similar prior work on the yeast enzyme. In view of the careful isotope effect studies of Parsons and co-workers [Goitein, R.K., Chelsky, D., & Parsons, S.M. (1978) J. Biol. Chem. 253, 2963-2971] and the results obtained by us, we propose that PRTases may involve a direct-transfer mechanism but with low bond order to the leaving pyrophosphate moiety and attacking base.",Nov 1990,"M B Bhatia, A Vinitsky, C Grubmeyer"
+945,90KWI/HUA,2157478.0,10.1021/bi00453a019,,['eng'],29,1,153-9,Biochemistry,"The kinetic reaction mechanism of the type II calmodulin-dependent protein kinase was studied by using its constitutively active kinase domain. Lacking regulatory features, the catalytic domain simplified data collection, analysis, and interpretation. To further facilitate this study, a synthetic peptide was used as the kinase substrate. Initial velocity measurements of the forward reaction were consistent with a sequential mechanism. The patterns of product and dead-end inhibition studies best fit an ordered Bi Bi kinetic mechanism with ATP binding first to the enzyme, followed by binding of the peptide substrate. Initial-rate patterns of the reverse reaction of the kinase suggested a rapid-equilibrium mechanism with obligatory ordered binding of ADP prior to the phosphopeptide substrate; however, this apparent rapid-equilibrium ordered mechanism was contrary to the observed inhibition by the phosphopeptide which is not supposed to bind to the kinase in the absence of ADP. Inspection of product inhibition patterns of the phosphopeptide with both ATP and peptide revealed that an ordered Bi Bi mechanism can show initial-rate patterns of a rapid-equilibrium ordered system when a Michaelis constant for phosphopeptide, Kip, is large relative to the concentration of phosphopeptide used. Thus, the results of this study show an ordered Bi Bi mechanism with nucleotide binding first in both directions of the kinase reaction. All the kinetic constants in the forward and reverse directions and the Keq of the kinase reaction are reported herein. To provide theoretical bases and diagnostic aid for mechanisms that can give rise to typical rapid-equilibrium ordered kinetic patterns, a discussion on various sequential cases is presented in the Appendix.",Jan 1990,"A P Kwiatkowski, C Y Huang, M M King"
+946,90LIU,,,,-,-,-,-,-,-,-,-
+947,90LIU/QUI,2139795.0,10.1021/bi00458a012,,['eng'],29,6,1417-25,Biochemistry,"Isochorismate synthase (EC 5.4.99.6), the entC gene product of Escherichia coli, catalyzes the conversion of chorismate to isochorismate, the first step in the biosynthesis of the powerful iron-chelating agent enterobactin. A sequence-specific deletion method has been used to construct an EntC overproducer, which allows for the purification and characterization of the E. coli isochorismate synthase for the first time. The N-terminal sequence and the subunit molecular weight (43,000) of the polypeptide derived from SDS-polyacrylamide gel electrophoresis agree with those deduced from DNA sequence data. The enzyme is an active monomer with a native molecular weight of 42,000. It was shown that EntC alone is fully capable of catalyzing the interconversion of chorismate and isochorismate in both directions and the associated activity is not affected by EntA of the same biosynthetic pathway as has recently been speculated [Elkins, M. F., & Earhart, C. F. (1988) FEMS Microbiol. Lett. 56, 35; Liu, J., Duncan, K., & Walsh, C.T. (1989) J. Bacteriol. 171, 791; Ozenberger, B. A., Brickman, T.J., & McIntosh, M. A. (1989) J. Bacteriol. 171, 775]. The kinetic constants were determined with Km = 14 microM and kcat = 173 min-1 for chorismate in the forward direction and Km = 5 microM and kcat = 108 min-1 for isochorismate in the backward direction. The equilibrium constant for the reaction derived from the kinetic data is 0.56 with the equilibrium lying toward the side of chorismate, corresponding to a free energy difference of 0.36 kcal/mol between chorismate and isochorismate.(ABSTRACT TRUNCATED AT 250 WORDS)",Feb 1990,"J Liu, N Quinn, G A Berchtold, C T Walsh"
+948,90LUN/APR,2140258.0,10.1042/bj2670739,,['eng'],267,3,739-43,The Biochemical journal,"The aim of this work was to use preparations from germinating seeds of Pisum sativum to determine the apparent equilibrium constant of the reaction catalysed by sucrose-phosphate synthase (EC 2.4.1.14) and to compare this with the mass-action ratio of the reaction in the seeds. The apparent equilibrium constant ranged from 5.3 at 0.25 mM-MgCl2, pH 7.0, to 62 at 10 mM-MgCl2, pH 7.5. The sucrose phosphate content of the seeds, 23 nmol/g fresh wt., was determined by separating sucrose phosphate from sucrose by ion-exchange chromatography and then measuring the sucrose released by alkaline phosphatase. Comparison of equilibrium constants and mass-action ratios in the cotyledons of 38 h-germinated seeds showed that the reactions catalysed by glucose-6-phosphate isomerase, phosphoglucomutase and UDP-glucose pyrophosphorylase are close to equilibrium, and those catalysed by sucrose-phosphate synthase and sucrose phosphatase are considerably displaced from equilibrium in vivo.",May 1990,"J E Lunn, T ap Rees"
+949,90OCO/BUT,,10.1016/0304-5102(90)85274-L,,-,-,-,-,-,-,-,-
+950,90SAN/SIN,2341161.0,,,['eng'],27,1,23-7,Indian journal of biochemistry & biophysics,"Phosphohexose isomerase from amyloplasts of immature wheat endosperm was purified 133-fold. The enzyme had a molecular weight of 130 kDa and maximum activity at pH 8.6. It showed normal hyperbolic kinetics for both fructose-6-P and glucose-6-P with Km of 0.12 mM and 0.44 mM, respectively. pH had a great influence on Km for fructose-6-P. Using glucose-6-P as the substrate, the equilibrium was reached at 23% fructose-6-P and 77% glucose-6-P and an equilibrium constant of about 3.0. The delta F calculated from the apparent equilibrium constant was +742 cal.mol-1. The activation energy calculated from the Arrhenius plot was 7450 cal.mol-1. None of the sulphydryl reagents at 2.5 mM concentration inactivated the enzyme. The enzyme was competitively inhibited by 6-phosphogluconate, ribose-5-P and ribulose-5-P with Ki values of 0.18, 0.14, and 0.13 mM, respectively. The probable role of the enzyme in starch biosynthesis in amyloplasts is discussed.",Feb 1990,"R S Sangwan, R Singh"
+951,91AND/KAT,,10.1021/ja00008a073,,-,-,-,-,-,-,-,-
+952,91GOL/BEL,1873473.0,10.1016/0301-4622(91)85030-t,,['eng'],40,1,69-76,Biophysical chemistry,"Microcalorimetry has been used to determine enthalpy changes for the hydrolysis of a series of oligosaccharides. High-pressure liquid chromatography was used to determine the extents of reaction and to check for any possible side reactions. The enzyme glucan 1,4-alpha-glucosidase was used to bring about the following hydrolysis reactions: (A) maltose(aq) + H2O(liq) = 2D-glucose(aq); (B) maltotriose(aq) + 2H2O(liq) = 3D-glucose(aq); (C) maltotetraose(aq) + 3H2O(liq) = 4D-glucose(aq); (D) maltopentaose(aq) + 4H2O(liq) = 5D-glucose(aq); (E) maltohexaose(aq) + 5H2O(liq) = 6D-glucose(aq); (F) maltoheptaose(aq) + 6H2O(liq) = 7D-glucose(aq); (G) amylose(aq) + nH2O(liq) = (n + 1) D-glucose(aq); and (H) panose(aq) + 2H2O(liq) = 3D-glucose(aq); (J) isomaltotriose(aq) + 2H2O(liq) = 3D-glucose(aq). The enzyme beta-fructofuranosidase was used for the reactions: (K) raffinose(aq) + H2O(liq) = alpha-D-melibiose(aq) + D-fructose(aq); and (L) stachyose(aq) + H2O(liq) = o-alpha-D-galactopyranosyl-(1----6)- alpha-o-D-galactopyranosyl-(1----6)-alpha-D-glucopyranose + D-fructose(aq). The results of the calorimetric measurements (298.15 K, 0.1 M sodium acetate buffer, pH 4.44-6.00) are: delta H0A = -4.55 +/- 0.10, delta H0B = -9.03 +/- 0.10, delta H0C = -13.79 +/- 0.15, delta H0D = -18.12 +/- 0.10, delta H0E = -22.40 +/- 0.15, delta H0F = -26.81 +/- 0.20, delta H0H = 1.46 +/- 0.40, delta H0J = 11.4 +/- 2.0, delta H0K = -15.25 +/- 0.20, and delta H0L = -14.93 +/- 0.20 kJ mol-1. The enthalpies of hydrolysis of two different samples of amylose were 1062 +/- 20 and 2719 +/- 100 kJ mol-1, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)",Apr 1991,"R N Goldberg, D Bell, Y B Tewari, M A McLaughlin"
+953,91HOR/UEH,,10.1271/bbb1961.55.1071,,-,-,-,-,-,-,-,-
+954,91HOR/WAT,,10.3109/10242429109000693,,-,-,-,-,-,-,-,-
+955,91KLE/RAN,,10.1093/jxb/42.4.537,,-,-,-,-,-,-,-,-
+956,91KNI/SEM,1645186.0,10.1021/bi00234a019,,['eng'],30,20,4970-7,Biochemistry,"A number of phosphorylated thiosugars have been prepared and tested as substrates for metabolic reactions. 6-Thioglucose-6-P is readily synthesized by reaction of 6-tosylglucose with trisodium thiophosphate at pH 10 in aqueous solution; the product has only sulfur between carbon and phosphorus. When ethyl glycerate is tosylated and treated similarly with thiophosphate, a 5:1 mixture of 3-thioglycerate-3-P and the 2-isomer is formed. 6-Thioglucose-6-P is converted by glycolytic enzymes to triose phosphates, 3-thioglycerol-3-P and 3-thioglycerate-3-P, and is oxidized by enzymes of the hexose monophosphate shunt to 5-thioribulose-5-P, which can be converted via phosphoribulokinase and ribulose-bis-P carboxylase into 3-P-glycerate and 3-thioglycerate-3-P. For most of the non-phosphoryl-transferring enzymes there are only moderate effects on Vmax and Km. Phosphoglucoisomerase, however, is very sensitive to the sulfur for oxygen change, with Vmax decreasing 60-fold and Km increasing 15-fold. Surprisingly, phosphoribulokinase has a V/K value for 5-thioribulose-5-P that is over 3 orders of magnitude less than for ribulose-5-P. 6-Thio-glucose-6-P was found to be a substrate for several enzymes that transfer the phosphoryl group. It is as good a substrate for alkaline phosphatase as glucose-6-P, and with phosphoglucomutase it is converted to 6-thioglucose-1-P with a rate that is 11% of the rate of reaction of glucose-1-P, with a Keq value of 45.6. The free energy of hydrolysis of the phosphorylated thiol is thus -7.2 kcal/mol at pH 7.(ABSTRACT TRUNCATED AT 250 WORDS)",May 1991,"W B Knight, D S Sem, K Smith, H M Miziorko, A R Rendina, W W Cleland"
+957,91KRA/GYG,,10.1002/anie.199108271,,-,-,-,-,-,-,-,-
+958,91LIU/FRO,1646815.0,10.1016/S0021-9258(18)99024-1,,['eng'],266,18,11774-8,The Journal of biological chemistry,"The enzymatic hydrolysis of fructose 1,6-bisphosphate (Fru-1,6-P2) to fructose 6-phosphate (Fru-6-P) and inorganic phosphate (Pi), which is catalyzed by fructose-1,6-bisphosphatase, has been studied by 31P nuclear magnetic resonance spectroscopy (NMR). At pH 7.5 and 15 degrees C, the equilibrium constant for the central complex K'eq = [E.Fru-6-P.Pi]/[E.Fru-1,6-P2.H2O] is about 2. This observation is in harmony with results obtained with a number of Bi Bi enzyme systems for the determination of K'eq in which a variety of experimental techniques were used (Knowles, J.R. (1980) Annu. Rev. Biochem. 49, 877-919). Significant changes in 31P NMR chemical shifts were observed for both the substrate, Fru-1,6-P2, and the product, Fru-6-P, when bound to the enzyme relative to ligand free in solution. The chemical shifts of the substrate and product were altered further in the presence of Mg2+, the catalytic divalent metal ion. The chemical shifts caused by the addition of metal ion can be reversed in the presence of trans-1,2-diaminocyclohexane- N,N,N',N'-tetraacetic acid (CDTA) or AMP. In the presence of the metal ion chelator or the nucleotide, the substrate had a chemical shift that was about the same as that observed in the absence of metal ion. On the basis of these observations we suggest that AMP and CDTA exhibit similar effects, i.e. they both remove the catalytic metal ion from the enzyme. This finding is supportive of the suggestion (Scheffler, J. E., and Fromm, H.J. (1986) Biochemistry 25, 6659-6665; Liu, F., and Fromm, H.J. (1990) J. Biol. Chem. 265, 7401-7406) that the role of AMP in the regulation of fructose-1,6-bisphosphatase is to prevent binding of the divalent metal activator to the enzyme.",Jun 1991,"F Liu, H J Fromm"
+959,91MOR/FRE,1653014.0,10.1021/bi00098a030,,['eng'],30,34,8494-500,Biochemistry,"The kinetic and thermodynamic parameters associated with the enzymatic reaction of yeast cytochrome c oxidase with its biological substrate, ferrocytochrome c, have been measured by using a titration microcalorimeter to monitor directly the rate of heat production or absorption as a function of time. This technique has allowed determination of both the energetics and the kinetics of the reaction under a variety of conditions within a single experiment. Experiments performed in buffer systems of varying ionization enthalpies allow determination of the net number of protons absorbed or released during the course of the reaction. For cytochrome c oxidase the intrinsic enthalpy of reaction was determined to be -16.5 kcal/mol with one (0.96) proton consumed for each ferrocytochrome c molecule oxidized. Activity measurements at salt concentrations ranging from 0 to 200 mM KCl in the presence of 10 mM potassium phosphate, pH 7.40, and 0.5 mM EDTA display a biphasic dependence of the electron transferase activity upon ionic strength with a peak activity observed near 50 mM KCl. The ionic strength dependence was similar for both detergent-solubilized and membrane-reconstituted cytochrome c oxidase. Despite the large ionic strength dependence of the kinetic parameters, the enthalpy measured for the reaction was found to be independent of ionic strength. Additional experiments involving direct transfer of the enzyme from low to high salt conditions produced negligible enthalpy changes that remained constant within experimental error throughout the salt concentrations studied (0-200 mM KCl). These results indicate that the salt effect on the enzyme activity is of entropic origin and further suggest the absence of a major conformational change in the enzyme due to changes in ionic strength.(ABSTRACT TRUNCATED AT 250 WORDS)",Aug 1991,"P E Morin, E Freire"
+960,91PAR/HOR,1939115.0,10.1016/S0021-9258(18)54759-1,,['eng'],266,31,20658-65,The Journal of biological chemistry,"Crithidia fasciculata cells grown on complex medium with added [8-14C, 5'-3H]inosine or [8-14C,5'-3H]adenosine metabolize greater than 50% of the salvaged nucleosides through a pathway involving N-glycoside bond cleavage. Cell extracts contain a substantial nucleoside hydrolase activity but an insignificant purine nucleoside phosphorylase. The nucleoside hydrolase has been purified 1000-fold to greater than 99% homogeneity from kilogram quantities of C. fasciculata. The enzyme is a tetramer of Mr 34,000 subunits to give an apparent holoenzyme Mr of 143,000 by gel filtration. All of the commonly occurring nucleosides are substrates. The Km values vary from 0.38 to 4.7 mM with purine nucleosides binding more tightly than the pyrimidines. Values of Vmax/Km vary from 3.4 x 10(3) M-1 s-1 to 1.7 x 10(5) M-1 s-1 with the pyrimidine nucleosides giving the larger values. The turnover rate for inosine is 32 s-1 at 30 degrees C. The kinetic mechanism with inosine as substrate is rapid equilibrium with random product release. The hydrolytic reaction can be reversed to give an experimental Keq of 106 M with H2O taken as unity. The product dissociation constants for ribose and hypoxanthine are 0.7 and 6.2 mM, respectively. Deoxynucleosides or 5'-substituted nucleosides are poor substrates or do not react, and are poor inhibitors of the enzyme. The enzyme discriminates against methanol attack from solvent during steady-state catalysis, indicating the participation of an enzyme-directed water nucleophile. The pH profile for inosine hydrolysis gives two apparent pKa values of 6.1 with decreasing Vmax/Km values below the pKa and a plateau at higher pH values. These effects are due to the pH sensitivity of the Vmax values, since Km is independent of pH. The pH profile implicates two negatively charged groups which stabilize a transition state with oxycarbonium character.",Nov 1991,"D W Parkin, B A Horenstein, D R Abdulah, B Estupiñán, V L Schramm"
+961,91SCH/GIF,,10.1016/0141-0229(91)90153-2,,-,-,-,-,-,-,-,-
+962,91SEM/CLE,1827991.0,10.1021/bi00234a020,,['eng'],30,20,4978-84,Biochemistry,"A number of phosphorylated aminosugars have been prepared and tested as substrates for metabolic reactions. 6-Aminoglucose is a slow substrate for yeast hexokinase with a Vmax that is only 0.012% that for glucose. While Vmax is pH independent, V/K decreases below the pK of 9.0 of the amino group. 6-Aminoglucose is a competitive inhibitor vs glucose with a Ki value increasing below the pK of 9 but leveling off at 33 mM below pH 7.16. Thus, protonation decreases binding affinity by 2.4 kcal/mol and only the neutral amine is catalytically competent. 6-Aminoglucose-6-P was synthesized enzymatically with hexokinase. Its pK's determined by 31P NMR were 2.46 and 8.02 (alpha anomer) and 2.34 and 7.85 (beta anomer), with a beta:alpha ratio of 3.0. It is most stable at pH 12 (half-life 228 h at 22 degrees C), while as a monoanion its half-life is 3 h. The free energy of hydrolysis at 25 degrees C and pH 9.25 is -10.3 kcal/mol. The phosphorylated amino analogues of 6-P-gluconate, ribulose-5-P, fructose-6-P, fructose-1,6-bis-P (amino group at C-6 only), and glyceraldehyde-3-P were synthesized enzymatically. The 31P NMR chemical shifts of these analogues are 8-8.5 ppm at pH 9.5. Their relative stability is 6-aminogluconate-6-P greater than 3-aminoglyceraldehyde-3-P greater than 6-aminoglucose-6-P greater than 6-aminofructose-1,6-bis-P congruent to 6-aminofructose-6-P greater than 5-aminoribulose-5-P. These analogues were tested as substrates for their respective enzymes.(ABSTRACT TRUNCATED AT 250 WORDS)",May 1991,"D S Sem, W W Cleland"
+963,91SRI/NAM,1873475.0,10.1016/0301-4622(91)85032-l,,['eng'],40,1,81-7,Biophysical chemistry,"Delta 1-Piperidine 2-carboxylic acid, an alpha-imino acid, is reduced by 1,4-dihydropyridines to pipecolic acid, an alpha-amino acid, and the corresponding pyridinium ions. This nonenzymatic reaction occurs only in the direction of pipecolic acid production. Glutamate dehydrogenase catalyzes this reaction when the reductant is NADPH and gives as products L-pipecolic acid and NADP+. The reaction velocity for the enzyme-catalyzed reaction is measurable in either direction. The pH-independent equilibrium constant, Keq, for the reduction of the imino acid by NADPH to give pipecolic acid anion and NADP+ was determined from the equilibrium conditions and the pKa values of pipecolic acid (10.72) and of the cyclic imino acid (8.10). The value of Keq was found to be 175 +/- 30; the values of delta G0, delta H0 and delta S0 are -3.1 +/- 0.1 kcal/mol, 5 +/- 1 kcal/mol and 27 +/- 4 e.u., respectively. The data indicate that the reactants are far more solvated than the products and that there must be a large degree of solvent reorganization during the course of the reaction. If these thermodynamic parameters apply to the redox step of the enzyme-catalyzed glutamate reaction, then the burst phase which results upon mixing the enzyme, L-glutamate and NADP+ in stoichiometric amounts must contain a hidden nonredox step of large delta H0 value to account for the curved Arrhenius plot observed for this phase (A.H. Colen, R.T. Medary and H.F. Fisher, Biopolymers 20 (1981) 879).",Apr 1991,"R Srinivasan, P Nambi"
+964,91TEW/GOL,1873472.0,10.1016/0301-4622(91)85029-p,,['eng'],40,1,59-67,Biophysical chemistry,"High-pressure liquid chromatography and microcalorimetry have been used to study the thermodynamics of the hydrolysis reactions of a series of disaccharides. The enzymes used to bring about the hydrolyses were: beta-galactosidase for lactulose and 3-o-beta-D-galactopyranosyl-D-arabinose; beta-glucosidase for alpha-D-melibiose; beta-amylase for D-trehalose; isomaltase for palatinose; and alpha-glucosidase for D-turanose. The buffer used was sodium acetate (0.02-0.10 M and pH 4.44-5.65). For the following processes at 298.15 K: lactulose(aq) + H2O(liq) = D-galactose(aq) + D-fructose(aq), K0 = 128 +/- 10 and delta H0 = 2.21 +/- 0.10 kJ mol-1; alpha-D-melibiose(aq) + H2O(liq) = D-galactose(aq) + D-glucose(aq), K0 = 123 +/- 42 and delta H0 = -0.88 +/- 0.50 kJ mol-1; palatinose(aq) + H2O(liq) = D-glucose(aq) + D-fructose(aq), delta H0 = -4.44 +/- 1.1 kJ mol-1; D-trehalose(aq) + H2O(liq) = 2 D-glucose(aq), K0 = 119 +/- 10 and delta H0 = 4.73 +/- 0.41 kJ mol-1; D-turanose(aq) + H2O(liq) = D-glucose(aq) + D-fructose(aq), delta H0 = -2.68 +/- 0.75 kJ mol-1; and 3-o-beta-D-galactopyranosyl-D-arabinose(aq) + H2O(liq) = D-galactose(aq) + D- arabinose(aq),0H0 = 107 +/- 10 and delta H0 = 2.97 +/- 0.10 kJ mol-1.(ABSTRACT TRUNCATED AT 250 WORDS)",Apr 1991,"Y B Tewari, R N Goldberg"
+965,91WOH/DIE,,10.1007/BF00243458,,-,-,-,-,-,-,-,-
+966,92BLA/GUI,,10.1002/bit.260400913,,-,-,-,-,-,-,-,-
+967,92DEM/ATT,,10.1016/S0232-4393(11)80392-6,,-,-,-,-,-,-,-,-
+968,92ELL/SRI,1540130.0,10.1042/bj2820155,,['eng'],282 ( Pt 1),Pt 1,155-64,The Biochemical journal,"1. The ratio of ebgA-gene product of ebgC-gene product in the functional aggregate of ebg beta-galactosidases was determined to be 1:1 by isolation of the enzyme from bacteria grown on uniformly radiolabelled amino acids and separation of the subunits by gel-permeation chromatography under denaturing conditions. 2. This datum, taken together with a recalculation of the previous ultracentrifuge data [Hall (1976) J. Mol. Biol. 107, 71-84], analytical gel-permeation chromatography and electron microscopy, strongly suggests an alpha 4 beta 4 quaternary structure for the enzyme. 3. The second chemical step in the enzyme turnover sequence, hydrolysis of the galactosyl-enzyme intermediate, is markedly slower for ebgab, having both Asp-97----Asn and Trp-977----Cys changes in the large subunit, than for ebga (having only the first change) and ebgb (having only the second), and is so slow as to be rate-determining even for an S-glycoside, beta-D-galactopyranosyl thiopicrate, as is shown by nucleophilic competition with methanol. 4. The selectivity of galactosyl-ebgab between water and methanol on a molar basis is 57, similar to the value for galactosyl-ebgb. 5. The equilibrium constant for the hydrolysis of lactose at 37 degrees C is 152 +/- 19 M, that for hydrolysis of allolactose is approx. 44 M and that for hydrolysis of lactulose is approx. 40 M. 6. A comparison of the free-energy profiles for the hydrolyses of lactose catalysed by the double mutant with those for the wild-type and the single mutants reveals that free-energy changes from the two mutations are not in general independently additive, but that the changes generally are in the direction predicted by the theory of Burbaum, Raines, Albery & Knowles [(1989) Biochemistry 28, 9283-9305] for an enzyme catalysing a thermodynamically irreversible reaction. 7. Michaelis-Menten parameters for the hydrolysis of six beta-D-galactopyranosylpyridinium ions and ten aryl beta-galactosides by ebgab were measured. 8. The derived beta 1g values are the same as those for ebgb (which has only the Trp-977----Cys change) and significantly different from those for ebgo (the wild-type enzyme) and ebga. 9. The alpha- and beta-deuterium secondary isotope effects on the hydrolysis of the galactosyl-enzyme of 1.08 and 1.00 are difficult to reconcile with the pyranose ring in this intermediate being in the 4C1 conformation.",Feb 1992,"A C Elliott, S K, M L Sinnott, P J Smith, J Bommuswamy, Z Guo, B G Hall, Y Zhang"
+969,92IBO/OBO,,10.3109/10242429209003660,,-,-,-,-,-,-,-,-
+970,92KAH/SCH,1527498.0,10.1099/00221287-138-6-1277,,['eng'],138,6,1277-81,Journal of general microbiology,"The phototrophic bacterium Rhodobacter sphaeroides strain Si4 induced ribitol dehydrogenase (EC 1.1.1.56) when grown on ribitol- or xylitol-containing medium. This ribitol dehydrogenase was purified to apparent homogeneity by ammonium sulphate precipitation, affinity chromatography on Procion red, and chromatography on Q-Sepharose. For the native enzyme an isoelectric point of pH 6.1 and an apparent M(r) of 50,000 was determined. SDS-PAGE yielded a single peptide band of M(r) 25,000 suggesting a dimeric enzyme structure. The ribitol dehydrogenase was specific for NAD+ but unspecific as to its polyol substrate. In order of decreasing activity ribitol, xylitol, erythritol, D-glucitol and D-arabitol were oxidized. The pH optimum of substrate oxidation was 10, and that of substrate reduction was 6.5. The equilibrium constant of the interconversion of ribitol to D-ribulose was determined to be 0.33 nM at pH 7.0 and 25 degrees C. The Km-values determined for ribitol, ribulose, xylitol and NAD+ (in the presence of ribitol) were 6.3, 12.5, 77 and 0.077 mM, respectively. Because of the favourable Km for ribitol, a method for quantitative ribitol determination was elaborated.",Jun 1992,"C Kahle, K H Schneider, F Giffhorn"
+971,92KEL/SCH,1318300.0,10.1016/S0021-9258(19)49761-5,,['eng'],267,17,11745-52,The Journal of biological chemistry,"Actinomycin synthetase I was purified to homogeneiety from actinomycin-producing Streptomyces chrysomallus. The purified enzyme is a single polypeptide chain of M(r) 45,000. It catalyzes the formation of the adenylate of 4-methyl-3-hydroxyanthranilic acid (4-MHA) from the free acid and ATP in an equilibrium reaction. 4-MHA is the precursor of the chromophoric part of actinomycin. By using the 4-MHA analogue, 4-methyl-3-hydroxybenzoic acid, as a model substrate it could be established that the equilibrium constant Keq is independent on enzyme concentration, which suggests that no stoichiometric acyladenylate-enzyme complex is formed in contrast to observations made with aminoacyl adenylates formed by aminoacyl-tRNA synthetases or multifunctional peptide synthetases. Actinomycin synthetase I does not charge itself with substrate carboxylic acid via a covalent thioester bond as is usual for amino acid activation in non-ribosomal peptide synthesis. In addition, the enzyme does not act as an acyl-coenzyme A ligase as revealed by its inability to release AMP in the presence of 4-MHA or other structurally related aromatic carboxylic acids, coenzyme A and ATP. Additional analysis of the activation reaction showed that it is exothermic, whereas the free enthalpy change delta G0 is positive due to a negative entropy change indicating a strong influence of restriction of random motion on the course of the reaction. Determinations of Km and kcat of various substrate carboxylic acids revealed the highest kcat/Km ratio for the natural substrate 4-MHA. From these properties, actinomycin synthetase I represents the prototype of novel chromophore activating enzymes involved in non-ribosomal synthesis of chromopeptide lactones in streptomycetes.",Jun 1992,"U Keller, W Schlumbohm"
+972,92KER/KER,,10.1016/0167-4838(92)90131-V,,-,-,-,-,-,-,-,-
+973,92KIM/KIN,,10.1152/ajpendo.1992.262.3.E344,,-,-,-,-,-,-,-,-
+974,92KIT/SAS,,10.1271/bbb.56.652,,-,-,-,-,-,-,-,-
+975,92KRA,,,,-,-,-,-,-,-,-,-
+976,92LEE/HAN,,,,-,-,-,-,-,-,-,-
+977,92LOR/TRA,,10.1016/B978-0-444-89046-7.50076-X,,-,-,-,-,-,-,-,-
+978,92QAM/YOO,1327136.0,10.1021/bi00156a018,,['eng'],31,41,9986-92,Biochemistry,"In order to define the overall kinetic mechanism of adenosine 3',5'-monophosphate dependent protein kinase catalytic subunit and also to elaborate the kinetic mechanism in the direction of peptide phosphorylation, we have determined its kinetic mechanism in the direction of MgADP phosphorylation. Studies of initial velocity as a function of uncomplexed Mg2+ (Mgf) in the absence and presence of dead-end inhibitors were used to define the kinetic mechanism. Data are consistent with the overall kinetic mechanism in the direction of MgADP phosphorylation being random with both the pathways allowed, i.e., the pathway in which MgADP binds to the enzyme prior to phosphorylated peptide and the pathway in which phosphorylated peptide binds to enzyme prior to MgADP. In addition, depending on the concentration of Mgf, one or the other pathway predominates. At low (0.5 mM) Mgf, the mechanism is steady-state ordered with the pathway in which phosphorylated peptide binds first being preferred; at high (10 mM) Mgf, the kinetic mechanism is equilibrium ordered, and the pathway in which MgADP binds first is preferred. This change in mechanism to equilibrium ordered at higher concentration of Mgf is due to an increase in affinity of the enzyme for MgADP and a decrease in affinity for the phosphorylated peptide. The Haldane relationship gives a Keq of 2 +/- 1 x 10(3) at pH 7.2, in agreement with the values obtained from 31P NMR (1.6 +/- 0.8 x 10(3)) and direct determination of reactant concentrations at equilibrium (3.5 +/- 0.6 x 10(3)).",Oct 1992,"R Qamar, M Y Yoon, P F Cook"
+979,92REK/TIS,,,,-,-,-,-,-,-,-,-
+980,92TEA/DOB,1629208.0,10.1016/S0021-9258(19)49682-8,,['eng'],267,20,14084-93,The Journal of biological chemistry,"The effect of temperature on the apparent equilibrium constant of creatine kinase (ATP:creatine N-phosphotransferase (EC 2.7.3.2)) was determined. At equilibrium the apparent K' for the biochemical reaction was defined as [formula: see text] The symbol sigma denotes the sum of all the ionic and metal complex species of the reactant components in M. The K' at pH 7.0, 1.0 mM free Mg2+, and ionic strength of 0.25 M at experimental conditions was 177 +/- 7.0, 217 +/- 11, 255 +/- 10, and 307 +/- 13 (n = 8) at 38, 25, 15, and 5 degrees C, respectively. The standard apparent enthalpy or heat of the reaction at the specified conditions (delta H' degree) was calculated from a van't Hoff plot of log10K' versus 1/T, and found to be -11.93 kJ mol-1 (-2852 cal mol-1) in the direction of ATP formation. The corresponding standard apparent entropy of the reaction (delta S' degree) was +4.70 J K-1 mol-1. The linear function (r2 = 0.99) between log10 K' and 1/K demonstrates that both delta H' degree and delta S' degree are independent of temperature for the creatine kinase reaction, and that delta Cp' degree, the standard apparent heat capacity of products minus reactants in their standard states, is negligible between 5 and 38 degrees C. We further show from our data that the sign and magnitude of the standard apparent Gibbs energy (delta G' degree) of the creatine kinase reaction was comprised mostly of the enthalpy of the reaction, with 11% coming from the entropy T delta S' degree term. The thermodynamic quantities for the following two reference reactions of creatine kinase were also determined. [formula: see text] The delta H degree for Reaction 2 was -16.73 kJ mol-1 (-3998 cal mol-1) and for Reaction 3 was -23.23 kJ mol-1 (-5552 cal mol-1) over the temperature range 5-38 degrees C. The corresponding delta S degree values for the reactions were +110.43 and +83.49 J K-1 mol-1, respectively. Using the delta H' degree of -11.93 kJ mol-1, and one K' value at one temperature, a second K' at a second temperature can be calculated, thus permitting bioenergetic investigations of organs and tissues using the creatine kinase equilibria over the entire physiological temperature range.",Jul 1992,"W E Teague, G P Dobson"
+981,92WAN/CHE,1633258.0,10.1016/0301-4622(92)80041-3,,['eng'],43,1,51-9,Biophysical chemistry,"The activity of acetylcholinesterase (AChE) in acetylcholine receptor (AChR)-enriched membrane vesicles isolated from electric organ of Torpedo californica exhibited a biphasic response to ethanol action. Below an ethanol concentration of 35 mM, AChE activity increased with increasing concentration of ethanol. At ethanol concentrations greater than 35 mM, the activity was found to decrease montonically. In contrast, ethanol (35-400 mM) increased the activity of soluble AChE. This biphasic behavior was consistent with the proposed important role of ethanol-membrane interaction. Microcalorimetric measurements revealed that the enthalpy change in acetylcholine (ACh) hydrolysis reaction was 586 J/mol in association with membrane-bound AChE in AChR-enriched membrane vesicles, as compared to -544 J/mol with the isolated soluble AChE. This discrepancy was attributed to the presence of membranes. Unlike its action on the enzyme activity, ethanol did not affect enthalpy change in ACh hydrolysis reaction catalyzed by either membrane-bound or soluble AChE. Comparison of results on activity and heat measurements suggested that the interaction of ethanol with membrane vesicles was nonspecific with no ethanol-induced membrane structural or conformational change.",May 1992,"Y Wang, C H Chen"
+982,92WED/LEY,8444866.0,10.1016/S0021-9258(18)53478-5,,['eng'],268,7,4880-8,The Journal of biological chemistry,"Isotope exchange kinetics at chemical equilibrium were used to probe the mechanisms of substrate binding and regulatory behavior of homoserine dehydrogenase-I from Escherichia coli. At pH 9.0, 37 degrees C, Keq = 100 (+/- 20) for the catalyzed reaction: L-aspartate-beta-semialdehyde + NADPH + H+ = L-homoserine + NADP+. Saturation curves for the exchange reactions, [14C]L-homoserine <--> L-aspartate-beta-semialdehyde and [3H]NADP+ <--> NADPH were observed as a function of different reactant-product pairs, varied in constant ratio at equilibrium. The NADP+ <--> NADPH exchange rate was inhibited upon variation of pairs involving L-aspartate-beta-semialdehyde and L-homoserine, consistent with preferred order random binding of cofactors before amino acids. Optimal rate constants, derived by simulations of equilibrium isotope exchange kinetics data with the ISOBI program, indicate faster dissociation of amino acids than cofactors from the central complexes but nearly equal rates for association of cofactors and amino acids to free enzyme. Rate limitation of net turnover in both directions is determined by dissociation of cofactor from the E-cofactor complex. The allosteric modifier, L-threonine, produces distinctive perturbations of the saturation curves for isotope exchange, which were analyzed systematically with the ISOBI program. The best fit to the data was obtained by L-threonine inhibiting catalysis between the central complexes without altering substrate association-dissociation rates. Simulations also showed that rate-limiting catalysis suppresses the kinetic inhibition effects that are characteristic of preferred order substrate binding, producing patterns typical for a (rapid equilibrium) random kinetic scheme.",Mar 1993,"F C Wedler, B W Ley"
+983,92WED/LEY1,1547269.0,10.1016/0167-4838(92)90209-V,,['eng'],1119,3,247-9,Biochimica et biophysica acta,"Isotope exchange kinetics at chemical equilibrium have been used to investigate the kinetic mechanism of homoserine dehydrogenase (EC 1.1.1.3) of the (Thr-sensitive) aspartokinase/homoserine dehydrogenase-I multifunctional enzyme from E. coli. For the reaction (L-ASA + NADPH + H+ = L-Hse + NADP+), at pH 9.0, 37 degrees C, Keq = 100 (+/- 20). Under these conditions, the rate for exchange of [14C]-L-homoserine (Hse) in equilibrium L-aspartate-beta-semialdehyde (ASA) is nearly twice that for the [3H]-NADP+ in equilibrium NADPH exchange. This indicates that covalent interconversion between reactants and products bound in the active site cannot be rate-limiting. Upon variation of the concentrations of all four substrates in constant ratio at equilibrium (to minimize dead-end complex formation), the Hse in equilibrium ASA exchange increased smoothly toward a maximum. In contrast, the NADP+ in equilibrium NADPH exchange rate increased to a maximum value at partial saturation, then decreased to approximately half the maximum rate. These data are consistent with a preferred-order random kinetic mechanism in which the dominant pathway involves association of NADPH prior to L-ASA and dissociation of L-Hse prior to NADP+.",Mar 1992,"F C Wedler, B W Ley, S L Shames, S J Rembish, D L Kushmaul"
+984,92XIA/XUE,,,,-,-,-,-,-,-,-,-
+985,93AND/BUL,8366124.0,10.1016/S0021-9258(19)36592-5,,['eng'],268,26,19858-65,The Journal of biological chemistry,"UDP-N-acetylglucosamine acyltransferase of Escherichia coli catalyzes the reaction, UDP-GlcNAc + R-3-hydroxymyristoyl-ACP--> UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc + ACP. Using Matrex Gel Green A and heparin-agarose, we have purified the enzyme to near homogeneity from a strain that overproduces it 474-fold. The subunit molecular mass determined by SDS-gel electrophoresis is approximately 30 kDa, consistent with results of previous radiolabeling experiments in mini-cells. The amino-terminal sequence (Met-Ile-Asp-Lys-Ser-Ala-Phe-Val-His-Pro) and the amino acid composition of the purified protein are consistent with DNA sequencing (Coleman, J., and Raetz, C. R. H. (1988) J. Bacteriol. 170, 1268-1274). At saturating concentrations of the second substrate, the apparent Km values for UDP-GlcNAc and R-3-hydroxymyristoyl-ACP are 99 and 1.6 microM, respectively. There is an absolute requirement for the R-3-hydroxy moiety of the fatty acyl-ACP substrate; myristoyl-ACP binds effectively (IC50 = 2 microM) but is inactive (< 0.01%) as an alternate substrate. The most remarkable feature of the reaction is its unfavorable equilibrium constant, Keq approximately equal to 0.01, which is not predicted by model S-->O acyl transfer reactions. Thus, although UDP-GlcNAc acyltransferase catalyzes the first unique step of lipid A biosynthesis, it is the second enzyme (the deacetylase) that commits the substrates to this pathway. The specific activity of the deacetylase is elevated approximately 5-fold when lipid A synthesis is inhibited.",Sep 1993,"M S Anderson, H G Bull, S M Galloway, T M Kelly, S Mohan, K Radika, C R Raetz"
+986,93BES/REB,8503876.0,10.1042/bj2920425,,['eng'],292 ( Pt 2),Pt 2,425-30,The Biochemical journal,"Plant tissues contain highly conjugated forms of folate. Despite this, the ability of plant folate-dependent enzymes to utilize tetrahydrofolate polyglutamates has not been examined in detail. In leaf mitochondria, the glycine-cleavage system and serine hydroxymethyltransferase, present in large amounts in the matrix space and involved in the photorespiratory cycle, necessitate the presence of tetrahydrofolate as a cofactor. The aim of the present work was to determine whether glutamate chain length (one to six glutamate residues) influenced the affinity constant for tetrahydrofolate and the maximal velocities displayed by these two enzymes. The results show that the affinity constant decreased by at least one order of magnitude when the tetrahydrofolate substrate contained three or more glutamate residues. In contrast, maximal velocities were not altered in the presence of these substrates. These results are consistent with analyses of mitochondrial folates which revealed a pool of polyglutamates dominated by tetra and pentaglutamates. The equilibrium constant of the serine hydroxymethyltransferase suggests that, during photorespiration, the reaction must be permanently pushed toward the formation of serine (the unfavourable direction) to allow the recycling of tetrahydrofolate necessary for the operation of the glycine decarboxylase T-protein.",Jun 1993,"V Besson, F Rebeille, M Neuburger, R Douce, E A Cossins"
+987,93BLI/MAR,,10.1016/0141-0229(93)90173-Y,,-,-,-,-,-,-,-,-
+988,93BOH/HUT,,10.1016/0040-6031(93)85092-N,,-,-,-,-,-,-,-,-
+989,93GOL/TEW,,10.1063/1.555939,,-,-,-,-,-,-,-,-
+990,93HUT/BOH,,10.1016/0040-6031(93)80327-7,,-,-,-,-,-,-,-,-
+991,93JAN/PAD,18613144.0,10.1002/bit.260420806,,['eng'],42,8,953-62,Biotechnology and bioengineering,"The lipase-catalyzed acylglycerol synthesis with fatty acids of different chain length is studied. Measured ester mole fractions at equilibrium are compared with calculated mole fractions. For these calculations the computer program TREP (Two-phase Reaction Equilibrium Prediction) is used. This program is based on the UNIFAC group contribution method and is developed for nondilute two-phase reaction systems.With one set of equilibrium constants, namely 1.3, 0.8, and 0.6 for monoester, diester, and triester synthesis, respectively, the equilibrium position of the reaction between glycerol and all saturated fatty acids with a chain length from 6 to 18 and oleic acid (cis-9-octadecenoic acid) can be calculated. Deviations, expressed as the ratio between calculated and measured ester mole fractions, usually were between 0.7 and 1.2. In the presence of solvents, the deviations of the monoester mole fractions were higher and rose up to 3. Without addition of a solvent, the ester mole fractions at equilibrium are dependent on the fatty acid chain length. With the short-chain hexanoic acid, the monoester mole fraction is the highest ester mole fraction, while for the long-chain oleic acid, the diester mole fraction is the highest one. The ester mole fractions become independent on the chain length of the fatty acid with a solvent added in a sufficient high concentration. Both reactions, with saturated and unsaturated C(18) fatty acids, lead to the same equilibrium position. The program TREP is found to make good predictions of the equilibrium amounts of ester and fatty acid. However, systematic deviations arise between measured and calculated amounts of water and glycerol in the organic phase. The calculated water and glycerol amounts are always lower than the measured ones. These deviations seem to be highest in nonpolar media and are probably due to deficiencies in the UNIFAC calculation method. Some preliminary experiments show the effect of the choice of solvent on the reaction rates. In polar solvents, the monoester production rate is enhances by a factor of 1.5 as compared to the reaction rate in a system without solvent.",Oct 1993,"A E Janssen, A Van der Padt, K V Riet"
+992,93LAR/TEW,,10.1006/jcht.1993.1009,,-,-,-,-,-,-,-,-
+993,93MOC/STR,,10.1016/S0031-9422(00)95139-2,,-,-,-,-,-,-,-,-
+994,93SHI/CHE,8381432.0,10.1016/S0021-9258(18)53720-0,,['eng'],268,5,3487-93,The Journal of biological chemistry,"Investigation on the biochemical isomerization of ibuprofen led us to the successful purification of ""2-arylpropionyl-CoA epimerase"" from rat liver cytosol and mitochondria. The purified enzymes from both subcellular fractions exhibit similar physical and catalytic properties and are distinctly different from rat liver methylmalonyl-CoA epimerase. Both are monomeric proteins with an apparent molecular mass of 42 kDa and show similar contents of most amino acids. Their UV spectra gave no indication of any bound cofactors, and their enzyme activities were not affected by exposure to EDTA or metal ions (except Cu2+). These results suggest that the cytosolic and mitochondrial epimerases may be structurally related. The purified enzymes catalyze the epimerization of various 2-arylpropionyl-CoAs with some degree of stereochemical differentiation. For 2-(4-isobutylphenyl)propionyl-CoA, the equilibrium constant was estimated to be 1.5 in favor of the R-isomer. Evidence indicated that the proton exchange may be mediated by a 2-base mechanism and that a carboxylic residue in the active site may serve as a general base for proton abstraction.",Feb 1993,"W R Shieh, C S Chen"
+995,93TEW/KIS,,10.1006/jcht.1993.1028,,-,-,-,-,-,-,-,-
+996,93VIN/GRU,7503993.0,10.1016/S0021-9258(19)74485-8,,['eng'],268,34,26004-10,The Journal of biological chemistry,"The pncB gene of Salmonella typhimurium was used to develop an overexpression system for nicotinate phosphoribosyltransferase (NAPRTase, EC 2.4.2.11), which forms nicotinate mononucleotide (NAMN) and PPi from nicotinate and alpha-D-5-phosphoribosyl-1-pyrophosphate (PRPP). NAPRTase hydrolyzes ATP in 1:1 molar stoichiometry to NAMN synthesis. Hydrolysis of ATP alters the ratio of products/substrates for the reaction nicotinate + PRPP <--> NAMN + PPi from its equilibrium value of 0.67 to a steady-state value of 1100. The energy for the maintenance of this ratio must come from ATP hydrolysis. However, in contrast to other ATP-utilizing enzymes, when all ATP is hydrolyzed the unfavorable product/substrate ratio collapses. ATP/ADP exchange results suggest that the overall reaction involves a phosphoenzyme (E-P) arising from E.ATP. Km values for nicotinate and PRPP each decreased by 200-fold when ATP was present to phosphorylate the enzyme. PPi stimulated the ATPase activity of the enzyme to Vmax values, suggesting that PPi formation during catalysis provides a trigger for cleavage of the putative E-P in the overall reaction and regenerates the low affinity form of the enzyme. A model is presented in which alternation of high and low affinity forms of NAPRTase provides a ""steady-state"" coupling between ATP hydrolysis and NAMN formation.",Dec 1993,"A Vinitsky, C Grubmeyer"
+997,93WER/TWE,16349034.0,10.1128/aem.59.9.2823-2829.1993,,['eng'],59,9,2823-9,Applied and environmental microbiology,"Maleate hydratase (malease) from Pseudomonas pseudoalcaligenes has been purified. The purified enzyme (98% pure) catalyzes the stereospecific addition of water to maleate and citraconate (2-methylmaleate), forming d-(+)-malate and d-(+)-citramalate, respectively. 2,3-Dimethylmaleate was also a substrate for malease. The stability of the enzyme was dependent on the protein concentration and the addition of dicarboxylic acids. The purified enzyme (89 kDa) consisted of two subunits (57 and 24 kDa). No cofactor was required for full activity of this colorless enzyme. Maximum enzyme activity was measured at pH 8 and 45 degrees C. The K(m) for maleate was 0.35 mM, and that for citraconate was 0.20 mM. Thiol reagents, such as p-chloromercuribenzoate and iodoacetamide, and sodium dodecyl sulfate completely inhibited malease activity. Malease activity was competitively inhibited by d-malate (K(i) = 0.63 mM) and d-citramalate (K(i) = 0.083 mM) and by the substrate analog 2,2-dimethylsuccinate (K(i) = 0.025 mM). The apparent equilibrium constants for the maleate, citraconate, and 2,3-dimethylmaleate hydration reactions were 2,050, 104, and 11.2, respectively.",Sep 1993,"M J van der Werf, W J van den Tweel, S Hartmans"
+998,93WER/TWE2,8223624.0,10.1111/j.1432-1033.1993.tb18332.x,,['eng'],217,3,1011-7,European journal of biochemistry,"Malease from Pseudomonas pseudoalcaligenes catalyses the hydration of both maleate and citraconate to D-malate and D-citramalate, respectively. The Kapp for these hydration reactions were 2050 and 104, respectively, under standard biochemical conditions (25 degrees C, pH 7.0, I = 0.1). The influence of the pH (6.0-8.5) on Kapp was determined. The Gibbs-free-energy changes under standard biochemical conditions for the hydration of the dianionic acids were calculated to be -19.28 kJ.mol-1 and -11.65 kJ.mol-1, respectively. From the obtained data together with data from the literature, the Gibbs free energy of formation of maleate2- and citraconate2- were calculated to be -588.91 kJ.mol-1 and -600.56 kJ.mol-1, respectively. The influence of the temperature (10-40 degrees C) on Kapp was determined for both hydration reactions. The enthalpy change (delta H degrees') and entropy change (delta S degrees') under standard biochemical conditions for the maleate2- (delta H degrees' = 18.07 kJ.mol-1, delta S degrees' = 2.94 J.mol-1 x K-1) and citraconate2- (delta H degrees' = -22.55 kJ.mol-1, delta S degrees' = -35.92 kJ.mol-1 x K-1) hydration reactions were calculated. The reaction rate of malease from Ps. pseudoalcaligenes was studied for both hydration reactions as a function of temperature. From these studies, the Gibbs free energies of activation for the maleate and citraconate hydration reactions catalysed by malease from Ps. pseudoalcaligenes were calculated to be 62.21 kJ.mol-1 and 63.43 kJ.mol-1, respectively.",Nov 1993,"M J van der Werf, W J van den Tweel, S Hartmans"
+999,93WIL/TOO,,10.1021/jo00065a010,,-,-,-,-,-,-,-,-
+1000,94CHI/KIR,,10.1016/0167-4838(94)90006-X,,-,-,-,-,-,-,-,-
+1001,94KIS/TEW,8155816.0,10.1016/0301-4622(93)e0067-f,,['eng'],49,2,163-74,Biophysical chemistry,"Apparent equilibrium constants and calorimetric enthalpies of reaction have been measured for the beta-lactamase catalyzed hydrolysis of penicillin G(aq) and ampicillin(aq) to penicillinoic acid(aq) and to ampicillinoic acid(aq), respectively. High-pressure liquid-chromatography and microcalorimetry were used to perform these measurements. The results for the reference reactions at T = 298.15 K and Im = 0 are: Ko = (9.4 +/- 3.1) x 10(-7), delta rGo = (34.4 +/- 1.0)kJ mol-1, delta rHo = -(73.7 +/- 0.4)kJ mol-1, and delta rSo = -(363 +/- 4) J K-1 mol-1 for penicillin G-(aq) + H2O(1) = penicillinoic acid2-(aq) + H+(aq); Ko = (6.0 +/- 3.0) x 10(-6), delta rGo = (29.8 +/- 1.7) kJ mol-1, delta rHo = -(70.0 +/- 7.5) kJ mol-1, and delta rSo = -(335 +/- 26) J K-1 mol-1 for ampicillin-(aq)+ H2O(1) = ampicillinoic acid2-(aq)+H+(aq). Calorimetric enthalpies of reaction for the beta-lactamase catalyzed hydrolysis of cephalosporin C have also been measured but the reaction products have not been identified and the measured enthalpies cannot be assigned to a specific reaction. Acidity constants for ampicillin, penicillin G, ampicillinoic acid, and penicillinoic acid are also reported. A strain energy of 116 kJ mol-1 for the beta-lactam ring is obtained from thermochemical data.",Mar 1994,"N Kishore, Y B Tewari, W T Yap, R N Goldberg"
+1002,94LEU/COO,8117730.0,10.1021/bi00175a040,,['eng'],33,9,2667-71,Biochemistry,"Serine transacetylase from Salmonella typhimurium was purified to near homogeneity. A complete initial velocity study in both reaction directions suggests that the enzyme catalyzes the conversion of acetyl CoA and L-serine to O-acetyl-L-serine (OAS) and coenzyme A (CoASH) by a ping pong bi bi kinetic mechanism. Initial velocity patterns in the absence of added inhibitors in both directions are best described by a series of parallel lines. Product inhibition by OAS is competitive with respect to acetyl CoA and noncompetitive with respect to L-serine, while product inhibition by L-serine is competitive against CoASH and noncompetitive against OAS. Glycine and S-methyl-L-cysteine (SMC) were used as dead-end analogs of L-serine and OAS, respectively. Glycine is competitive against L-serine, and uncompetitive against acetyl CoA, while SMC is competitive against OAS and uncompetitive against CoASH. All of the above inhibition patterns are consistent with those predicted for a single site ping pong bi bi kinetic mechanism. The equilibrium constant for the transacetylase reaction is 15 in the direction of serine acetylation. The constant was measured by monitoring the change in CoASH concentration obtained for reactions in which the ratio of acetyl CoA/CoASH was constant and the ratio of OAS/serine was varied. The Keq calculated from the Haldane relationship is in good agreement with the value obtained by direct measurement.",Mar 1994,"L S Leu, P F Cook"
+1003,94NOE/COL,,10.1016/S0885-5765(05)80059-1,,-,-,-,-,-,-,-,-
+1004,94REK/SCH,,10.1021/j100066a032,,-,-,-,-,-,-,-,-
+1005,94TEW/GOL,,10.1007/BF00973544,,-,-,-,-,-,-,-,-
+1006,95BIS/KRA,,10.1002/9783527619429.ch4,,-,-,-,-,-,-,-,-
+1007,95CHE/ARM,,10.1021/tx00046a012,,-,-,-,-,-,-,-,-
+1008,95GOL/TEW,,10.1063/1.555969,,-,-,-,-,-,-,-,-
+1009,95HUT/BOH,,10.1016/0040-6031(94)01957-I,,-,-,-,-,-,-,-,-
+1010,95JUS/KOT,,10.1016/0040-6031(95)90714-9,,-,-,-,-,-,-,-,-
+1011,95KAM/JUR,,10.1007/BF00301478,,-,-,-,-,-,-,-,-
+1012,95KOZ/TOM,,10.1021/ja00113a002,,-,-,-,-,-,-,-,-
+1013,95LEE/WAL,,10.1021/ja00133a006,,-,-,-,-,-,-,-,-
+1014,95LIA/WAN,,,,-,-,-,-,-,-,-,-
+1015,95LIA/WAN2,,10.1016/0040-6031(95)02513-8,,-,-,-,-,-,-,-,-
+1016,95LIU/ZEN,,10.1016/0040-6031(94)02080-8,,-,-,-,-,-,-,-,-
+1017,95PEL/MAC,7548019.0,10.1021/bi00039a025,,['eng'],34,39,12673-80,Biochemistry,"The bifunctional dehydrogenase/cyclohydrolase domain of the human NADP-dependent trifunctional methyleneH4folate dehydrogenase/methenylH4folate cyclohydrolase/formylH4folate synthetase (H4folate = tetrahydrofolate) catalyzes two sequential reactions involved in the interconversion of H4folate derivatives. We have established by equilibrium dialysis that a single H4folate-binding site exists per monomer of the dimeric domain and that the presence of nucleotides has two unexpected effects on H4folate substrate binding. Nucleotides containing a 5'-phosphate cause positive cooperativity in the binding of methyleneH4folate but not of 10-formylH4folate, and NADP increases the affinity for 10-formylH4folate by a factor of 25. The results indicate that dinucleotide preferentially binds before 10-formylH4folate in the reverse cyclohydrolase reaction, and this mechanism increases the efficiency of conversion of 10-formylH4folate to methyleneH4folate. We report new kinetic data that are also consistent with a steady-state random mechanism for this enzyme. To assess whether the enzyme functions at equilibrium in vivo, we determined the overall chemical equilibrium constant of Keq = 16 for ([10- formylH4folate][NADPH])/([methyleneH4folate][NADP]). Using this value and reported ratios of free dinucleotides and folate derivatives in vivo, we estimate that the cytosolic dehydrogenase/cyclohydrolase reactions exist near the equilibrium position. However, the NAD-dependent dehydrogenase/cyclohydrolase reactions in mitochondria are far from equilibrium and are poised toward 10-formylH4folate synthesis. The results of the binding and kinetic studies indicate that the bifunctional nature of the methyleneH4folate dehydrogenase/methenylH4folate cyclohdrolase domain is designed to optimize the overall reverse reactions in vivo.",Oct 1995,"J N Pelletier, R E MacKenzie"
+1018,95SCH/TRA,7827041.0,10.1021/bi00003a016,,['eng'],34,3,824-32,Biochemistry,"The structure of the key glycolytic enzyme 3-phosphoglycerate kinase (PGK) is known in detail, but there is little information on its reaction pathway. We have studied its equilibrium and transient kinetics in the direction of 1,3-bisphosphoglycerate (1,3-bis-P-glycerate) production: ATP + 3-P-glycerate<==>ADP + 1,3-bis-P-glycerate. We devised a sensitive method for following this production. PGK is mixed with 3-P-glycerate and [gamma-32P]ATP in a rapid flow quench apparatus. The reaction mixtures are aged for 4 ms or more and then quenched in acid in which any [1-32P]-1,3-P-glycerate decomposes to 3-P-glycerate and 32Pi, which is determined specifically. The Pi reflects accurately the 1,3-bis-P-glycerate in the original reaction mixture, and the kcat obtained is identical to that obtained by the conventional linked assay method with glyceraldehyde-3-phosphate dehydrogenase. This does not support the postulate of a rapid direct transfer of the 1,3-bis-P-glycerate between the kinase and the dehydrogenase [Srivastava, D. K., & Bernhard, S. A. (1986) Science 234, 1081-1086]. We fitted our data to a simple scheme with the formation of binary complexes, the interconversion of substrates to products via ternary complexes, and the release of products. Because of the high turnover of PGK, the work was carried out under cryoenzymic conditions with 40% ethylene glycol in the buffer. The glycol decreased kcat from 80 to 8.5 s-1 (pH 7.5, 4 degrees C), but the Km for 3-P-glycerate and ATP and the equilibrium constants in the scheme were little affected. We carried out two types of experiment.(ABSTRACT TRUNCATED AT 250 WORDS)",Jan 1995,"P P Schmidt, F Travers, T Barman"
+1019,95TEW/SCH,,10.1021/j100005a034,,-,-,-,-,-,-,-,-
+1020,95WIS/KUS,7759484.0,10.1074/jbc.270.21.12428,,['eng'],270,21,12428-38,The Journal of biological chemistry,"The hypothesis tested was whether creatine kinase (CK) equilibrates with its substrates and products in the cytosol as if in solution. We used the creatine analogs cyclocreatine (cCr) or beta-guanidopropionate (beta GPA) to test if mass action ratios (gamma) for CK in muscle could be predicted from combined equilibrium constants (Kcomb) measured in solutions mimicking the intracellular environment. Mice were fed cCr or beta GPA and their muscles assayed for substrates and products of the CK reaction by 31P NMR spectroscopy and high performance liquid chromatography. After three weeks of feeding, gamma was indistinguishable from Kcomb in cCr-treated muscles demonstrating both PCr/Cr and phospho-analog/analog must have equilibrated with a constant and uniform cellular ATP/ADP ratio. In beta GPA-treated muscles, gamma was smaller than Kcomb due to a higher content of muscle beta GPA. Feeding beta GPA for 9-12 weeks resulted in a closer agreement between Kcomb and gamma, suggesting ATP/ADP ratios are not uniform within the muscle perhaps due to transient metabolic stress in some cells. From this analysis it follows that calculation of free ADP from the CK equilibrium for a heterogeneous population of cells with respect to total Cr and ATP content is correct only if chemical potentials of these cells are uniform.",May 1995,"R W Wiseman, M J Kushmerick"
+1021,96ARA/RUZ,8639492.0,10.1021/bi952983w,,['eng'],35,11,3426-8,Biochemistry,"The reversible reaction of UDP-glucose with imidazole (Im) to produce uridine 5'-phoshoimidazolate (UMPIm) and glucose-1-P is catalyzed by UDP-hexose synthase, which is the mutant H166G of hexose-1-P uridylyltransferase (EC 2.7.7.12) [Kim, J., Ruzicka, F.J., & Frey, P.A. (1990) Biochemistry 29, 10590-10593]. The availability of UDP-hexose synthase allows the equilibrium constant for the reaction UDP-glucose + Im = UMPIm + glucose-1-P to be measured, and it is found to be 2.2 x 10(-2) at pH 8.5 and 27 degrees C. At pH 7.0 and 27 degrees C the equilibrium constant is 6.4 x 10(-4). The equilibrium constant for the formation of the covalent uridylyl-enzyme intermediate of hexose-1-P uridylyltransferase (E-His(166) + UDP-glucose = E-His(166)-UMP + glucose-1-P) is found to be 1.8 x 10(-4) at pH 7.0 and 25 degrees C, which is slightly less favorable than the formation of UMPIm from UDP-glucose and Im. These equilibrium constants, when considered in the light of other data in the literature, allow the standard free energy changes for the hydrolysis of UMPIm and the analogous covalent uridylyl-enzyme intermediate to be calculated. The results show that delta G' degrees (delta G degrees (ph)(7.0)) for the hydrolyses of UMPIm and E-His(166)-UMP are -14.7 and -15.4 kcal mol(-1), respectively at pH 7.0. At pH 8.5, the corresponding values of delta G degrees (ph) (8.5) are -12.6 and -9.9 kcal mol(-1), respectively. It is concluded that noncovalent binding interactions between the active site and the UMP group of E-His(166)-UMP provide little or no stabilization in the formation of this species as an intermediate in the reaction of hexose-1-P uridylyltransferase.",Mar 1996,"A Arabshahi, F J Ruzicka, S Geeganage, P A Frey"
+1022,96HIR/MAY,,10.5650/jos1996.45.761,,-,-,-,-,-,-,-,-
+1023,96KIM/DUN,8605214.0,10.1021/bi952944k,,['eng'],35,14,4628-35,Biochemistry,"Phosphoenolpyruvate phosphomutase (PEP mutase) from Tetrahymena pyriformis catalyzes the rearrangement of phosphoenolpyruvate (PEP) to phosphonopyruvate (P-pyr). A spectrophotometric P-pyr assay consisting of the coupled actions of P-pyr decarboxylase, phosphonoacetaldehyde hydrolase, and alcohol dehydrogenase was devised to monitor mutase catalysis. The reaction constants determined for PEP mutase catalyzed conversion of PEP to P-pyr at pH 7.5 and 25 degrees C in the presence of Mg(II) are kcat = 5 s(-1), Km = 0.77 +/- 0.05 mM, and Keq = (2-9) x 10(-4). In the PEP forming direction, kcat = 100 s(-1) and Km = 3.5 +/- 0.1 microM. Retention of stereochemistry at phosphorus and strong inhibition displayed by the pyruvyl enolate analog, oxalate, have been cited as two lines of evidence that PEP mutase catalysis proceeds via a phosphoenzyme-pyruvyl enolate intermediate [Seidel, H. M., & Knowles, J. R. (1994) Biochemistry 33, 5641-5646]. In this study, single turnover reactions of oxalyl phosphate with the PEP mutase were carried out to test the formation of the phosphoenzyme intermediate. If formed. the phosphoenzyme-oxalate complex should be sufficiently stable to isolate. Reaction of the mutase with [32P]oxalyl phosphate in the presence of Mg(II)/Mn(II) cofactor failed to produce a detectable level of the [32P]phosphoenzyme-oxalate complex. In contrast, the same reaction carried out with pyruvate phosphate dikinase (PPDK), an enzyme known to catalyze the phosphorylation of its active site histidine with PEP, occurred at a rate of 4 x 10(-4) s(-1) (15% E-P formed) in the presence Mg(II) and at a rate of 3 x 10(-3) s(-1) (60% E-P formed) in the presence of Mn(II). Both oxalyl phosphate (Ki = 180 +/- 10 microM) and oxalate (Ki = 32 +/- 1O microM) were competitive inhibitors of PEP mutase catalysis, but neither displayed slow, tight binding inhibition. These results do not support the intermediacy of a phosphoenzyme-pyruvyl enolate complex in PEP mutase catalysis.",Apr 1996,"J Kim, D Dunaway-Mariano"
+1024,96LI/ZHA,8910414.0,10.1074/jbc.271.45.28038,,['eng'],271,45,28038-44,The Journal of biological chemistry,"Yeast guanylate kinase was expressed at high level in Escherichia coli using pET-17b vector. It was purified to homogeneity by a simple two-column procedure with an average yield of approximately 100 mg/liter. The steady-state kinetic parameters for both forward and reverse reactions were determined by initial velocity measurements. The turnover numbers (kcat) were 394 s-1 for the forward reaction (formation of ADP and GDP) and 90 s-1 for the reverse reaction (formation of ATP and GMP). Km values were 0.20, 0. 091, 0.017, and 0.097 mM for MgATP, GMP, MgADP, and GDP, respectively. Analysis of the initial velocity patterns indicated a sequential mechanism. GMP was found to have partial substrate inhibition. The substrate inhibition was not competitive with MgATP and could be attributed to formation of the abortive complex guanylate kinase.MgADP.GMP. The equilibrium constant of the reaction was measured under various conditions by NMR and a radiometric assay. The results showed that the steady-state kinetic parameters were consistent with the thermodynamic constant. NMR titration and equilibrium dialysis showed that both substrates and products could bind to free guanylate kinase. The dissociation constants were 0.090, 0.18, 0.029, 0.084, and 0.12 mM for MgATP, ATP, GMP, MgADP, and GDP, respectively. Viscosity-dependent kinetics was used to identify the rate-limiting steps of the reaction. The results indicated that the reaction rate is largely controlled by the chemical step.",Nov 1996,"Y Li, Y Zhang, H Yan"
+1025,96LIA/WAN,,,,-,-,-,-,-,-,-,-
+1026,96OES/SCH,,10.1016/S0168-9452(96)04475-5,,-,-,-,-,-,-,-,-
+1027,96PRO/GRO,,10.1111/j.1399-3054.1996.tb06681.x,,-,-,-,-,-,-,-,-
+1028,96TEW/GOL,,10.1006/jcht.1996.0099,,-,-,-,-,-,-,-,-
+1029,96TEW/SCH,,10.1006/jcht.1996.0016,,-,-,-,-,-,-,-,-
+1030,97CHA,9326504.0,10.1242/jeb.200.21.2789,,['eng'],200,Pt 21,2789-96,The Journal of experimental biology,"Mitochondria isolated from the posterior midgut of the tobacco hornworm (Manduca sexta) contain arginine kinase. The distribution of mitochondrial and cytoplasmic marker enzymes indicates that the presence of mitochondrial arginine kinase is not due to cytoplasmic contamination. Arginine is not oxidized by the midgut mitochondria but, when metabolic substrates and ATP are present, respiration can be initiated by the addition of arginine. Under these conditions, there is no return to State 4 respiration, indicating regeneration of ADP by the arginine kinase reaction. Respiration can be blocked, however, by atractyloside, an inhibitor of the adenine nucleotide translocator. These results indicate that arginine kinase resides outside the matrix. Mitochondrial arginine kinase is specific to l-arginine since analogs of l-arginine are ineffective in stimulating respiration in the presence of ATP. Coupling between the adenine nucleotide translocator and arginine kinase was investigated using kinetic and thermodynamic approaches. There were no differences in the activities of arginine kinase in respiring and non-respiring mitochondria when they were measured at different ATP or arginine concentrations. This result indicates that arginine kinase does not have preferential access to the ATP exported out of the matix. A comparison of the apparent equilibrium constant and the mass action ratio of the arginine kinase reaction also confirms that there is no microcompartmentation of the reaction.", 1997,M Chamberlin
+1031,97CON/DEL,,10.1016/S0141-0229(97)00021-5,,-,-,-,-,-,-,-,-
+1032,97DEJ/ROC,,10.1007/BF01007697,,-,-,-,-,-,-,-,-
+1033,97HAN/KLE,,10.1016/S0167-4838(96)00161-6,,-,-,-,-,-,-,-,-
+1034,97KAS/TEW,,10.1021/jp972501l,,-,-,-,-,-,-,-,-
+1035,97LIA/WU,,10.1016/S0040-6031(97)00363-8,,-,-,-,-,-,-,-,-
+1036,97PES/PRI,,10.1002/(SICI)1097-0290(19971005)56:1<9::AID-BIT2>3.0.CO,,-,-,-,-,-,-,-,-
+1037,97SAL/GOD,,10.1021/bp9700869,,-,-,-,-,-,-,-,-
+1038,97STA/SUA,9319107.0,10.1242/jeb.200.8.1247,,['eng'],200,Pt 8,1247-54,The Journal of experimental biology,"In honeybee flight muscle, there are close matches between physiological flux rates and the maximal activities (Vmax; determined using crude homogenates) of key enzymes catalyzing non-equilibrium reactions in carbohydrate oxidation. In contrast, phosphoglucose isomerase (PGI), which catalyzes a reaction believed to be close to equilibrium, occurs at Vmax values greatly in excess of glycolytic flux rates. In this study, we measure the Vmax of flight muscle PGI, the kinetic parameters of the purified enzyme, the apparent equilibrium constants for the reaction and the tissue concentrations of substrate and product. Using the Haldane equation, we estimate that the forward flux capacity (Vf) for PGI required to achieve physiological glycolytic flux rates is between 800 and 1070 units ml-1 cell water, approximately 4560 % of the empirically measured Vmax of 1770 units ml-1 cell water at optimal pH (8.0) and low ionic strength (no added KCl). When measured at physiological pH (7.0) and ionic strength (120 mmol l-1 KCl) with saturating levels of substrate, PGI activity is 1130 units ml-1 cell water, a value close to the calculated Vf. These results reveal a very close match between predicted and measured PGI flux capacities, and support the concept of an economical design of muscle metabolism in systems working at very high metabolic rates.", 1997,"J Staples, R Suarez"
+1039,97TEW/GOL,,10.1016/S0008-6215(97)00073-6,,-,-,-,-,-,-,-,-
+1040,97XU/EAD,9132023.0,10.1021/bi9616007,,['eng'],36,12,3700-12,Biochemistry,"Hypoxanthine-guanine phosphoribosyltransferase (HGPRTase) is the locus of Lesch-Nyhan syndrome, the activator of the prodrugs 6-mercaptopurine and allopurinol, and a target for antiparasitic chemotherapy. The three-dimensional structure of the recombinant human enzyme in complex with GMP has recently been solved [Eads, J., Scapin, G., Xu, Y., Grubmeyer, C., & Sacchettini, J. C. (1994) Cell 78, 325-334]. Here, ligand binding, pre-steady state kinetics, isotope trapping, and isotope exchange experiments are presented which detail the sequential kinetic mechanism of the enzyme. In the forward reaction, in which a base (hypoxanthine or guanine) reacts with PRPP to form nucleoside monophosphate and PPi, binding of PRPP precedes that of the base, and in the reverse direction, IMP binds first. Compared to k(cat), phosphoribosyl group transfer is rapid in both the forward (131 vs 6.0 s(-1)) and reverse (9 vs 0.17 s(-1)) directions. In the forward direction, product pyrophosphate dissociates rapidly (> 12 s(-1)) followed by release of IMP (6.0 s(-1)). In the reverse direction, Hx dissociates rapidly (9.5 s(-1)) and PRPP dissociates slowly (0.24 s(-1)). The more rapid rate of utilization of guanine than hypoxanthine in the forward reaction is the result of the faster release of product GMP rather than the result of differences in the rate of the chemical step. The kinetic mechanism, with rapid chemistry and slow product dissociation, accounts for the previously observed ability of the alternative product guanine to stimulate, rather than inhibit, the pyrophosphorolysis of IMP. The overall equilibrium for the hypoxanthine phosphoribosyl transfer reaction lies far toward nucleotide product (Keq approximately 1.6 x 10(5)), at the high end for PRPP-linked nucleotide formation. The three-dimensional structure of the HGPRTase x IMP complex has been solved to 2.4 A resolution and is isomorphous with the GMP complex. The results of the ligand binding and kinetic studies are discussed in light of the structural data.",Mar 1997,"Y Xu, J Eads, J C Sacchettini, C Grubmeyer"
+1041,97YOR/ISH,,10.1093/oxfordjournals.jbchem.a021786,,-,-,-,-,-,-,-,-
+1042,98CON/BOR,,10.1007/s004490050406,,-,-,-,-,-,-,-,-
+1043,98CON/DEL,,10.1007/s004490050406,,-,-,-,-,-,-,-,-
+1044,98DIE/STR,,10.1016/S1381-1177(98)00044-7,,-,-,-,-,-,-,-,-
+1045,98DIE/STR2,,10.3109/10242429809003622,,-,-,-,-,-,-,-,-
+1046,98KIM/VOE,9506987.0,10.1074/jbc.273.12.6844,,['eng'],273,12,6844-52,The Journal of biological chemistry,"In the yeast Saccharomyces cerevisiae, choline kinase (ATP:choline phosphotransferase, EC 2.7.1.32) is the product of the CKI gene. Choline kinase catalyzes the committed step in the synthesis of phosphatidylcholine by the CDP-choline pathway. The yeast enzyme was overexpressed 106-fold in Sf-9 insect cells and purified 71.2-fold to homogeneity from the cytosolic fraction by chromatography with concanavalin A, Affi-Gel Blue, and Mono Q. The N-terminal amino acid sequence of purified choline kinase matched perfectly with the deduced sequence of the CKI gene. The minimum subunit molecular mass (73 kDa) of purified choline kinase was in good agreement with the predicted size (66.3 kDa) of the CKI gene product. Native choline kinase existed in oligomeric structures of dimers, tetramers, and octomers. The amounts of the tetrameric and octomeric forms increased in the presence of the substrate ATP. Antibodies were raised against the purified enzyme and were used to identify choline kinase in insect cells and in S. cerevisiae. Maximum choline kinase activity was dependent on Mg2+ ions (10 mM) at pH 9.5 and at 30 degrees C. The equilibrium constant (0.2) for the reaction indicated that the reverse reaction was favored in vitro. The activation energy for the reaction was 6.26 kcal/mol, and the enzyme was labile above 30 degrees C. Choline kinase exhibited saturation kinetics with respect to choline and positive cooperative kinetics with respect to ATP (n = 1.4-2.3). Results of the kinetic experiments indicated that the enzyme catalyzes a sequential Bi Bi reaction. The Vmax for the reaction was 138.7 micromol/min/mg, and the Km values for choline and ATP were 0.27 mM and 90 microM, respectively. The turnover number per choline kinase subunit was 153 s-1. Ethanolamine was a poor substrate for the purified choline kinase, and it was also poor inhibitor of choline kinase activity. ADP inhibited choline kinase activity (IC50 = 0.32 mM) in a positive cooperative manner (n = 1.5), and the mechanism of inhibition with respect to ATP and choline was complex. The regulation of choline kinase activity by ATP and ADP may be physiologically relevant.",Mar 1998,"K H Kim, D R Voelker, M T Flocco, G M Carman"
+1047,98KIS/TEW,9700925.0,10.1016/s0301-4622(98)00151-3,,['eng'],73,3,265-80,Biophysical chemistry,"Microcalorimetry and high-performance liquid chromatography have been used to conduct a thermodynamic investigation of the following reactions catalyzed by the tryptophan synthase alpha 2 beta 2 complex (EC 4.2.1.20) and its subunits: indole(aq) + L-serine(aq) = L-tryptophan(aq) + H2O(1); L-serine(aq) = pyruvate(aq) + ammonia(aq); indole(aq) + D-glyceraldehyde 3-phosphate(aq) = 1-(indol-3-yl)glycerol 3-phosphate(aq); L-serine(aq) + 1-(indol-3-yl)glycerol 3-phosphate(aq) = L-tryptophan(aq) + D-glyceraldehyde 3-phosphate(aq) + H2O(1). The calorimetric measurements led to standard molar enthalpy changes for all four of these reactions. Direct measurements yielded an apparent equilibrium constant for the third reaction; equilibrium constants for the remaining three reactions were obtained by using thermochemical cycle calculations. The results of the calorimetric and equilibrium measurements were analyzed in terms of a chemical equilibrium model that accounted for the multiplicity of the ionic states of the reactants and products. Thermodynamic quantities for chemical reference reactions involving specific ionic forms have been obtained. These quantities permit the calculation of the position of equilibrium of the above four reactions as a function of temperature, pH, and ionic strength. Values of the apparent equilibrium constants and standard transformed Gibbs free energy changes delta r G'(m) degree under approximately physiological conditions are given. Le Châtelier's principle provides an explanation as to why, in the metabolic pathway leading to the synthesis of L-tryptophan, the third reaction proceeds in the direction of formation of indole and D-glyceraldehyde 3-phosphate even though the apparent equilibrium constant greatly favors the formation of 1-(indol-3-yl)glycerol 3-phosphate.",Jul 1998,"N Kishore, Y B Tewari, D L Akers, R N Goldberg, E W Miles"
+1048,98KIS/TEW2,,10.1006/jcht.1998.0404,,-,-,-,-,-,-,-,-
+1049,98LAE/EIS,9738901.0,10.1046/j.1432-1327.1998.2550618.x,,['eng'],255,3,618-27,European journal of biochemistry,"Many aromatic compounds can be metabolized by bacteria under anoxic conditions via benzoyl-CoA as the common intermediate. The central pathway of benzoyl-CoA metabolism is initiated by an ATP-driven reduction of the aromatic ring producing cyclohexa-1,5-diene-1-carbonyl-CoA. The 1,5-dienoyl-CoA intermediate is thought to be transformed to 6-hydroxycyclohex-1-ene-1-carbonyl-CoA by a specific dienoyl-CoA hydratase catalyzing the formal addition of water to one of the double bonds. This dienoyl-CoA hydratase was detected in the denitrifying bacterium Thauera aromatica after anaerobic growth with benzoate. Substrate and product were confirmed and a convenient spectrophotometric assay was developed. The equilibrium concentrations of substrate and product were almost equal. Enzyme activity was induced after anoxic growth with benzoate, in contrast to acetate. The enzyme of 28 kDa was purified from T. aromatica and was found to be highly specific for the cyclic 1,5-dienoyl-CoA. A second 29-kDa enoyl-CoA hydratase acted on crotonyl-CoA; this highly active enoyl-CoA hydratase also acted slowly on cyclohex-1-ene-1-carbonyl-CoA. The regulation of expression of dienoyl-CoA hydratase activity, the kinetic constants, the substrate specificity, and the specific activity of the enzyme in cell extract provide evidence that dienoyl-CoA hydratase is the second enzyme of the central benzoyl-CoA pathway of anaerobic aromatic metabolism in T. aromatica. Extracts of Rhodopseudomonas palustris contained high activity of cyclohex-1-ene-1-carbonyl-CoA hydratase, but no 1,5-dienoyl-CoA hydratase activity. It appears that a variant of the benzoyl-CoA pathway is operating in R. palustris in which hydration of the 1,5-dienoyl-CoA does not take place. Rather, cyclohex-1-ene-1-carbonyl-CoA is hydrated to 2-hydroxycyclohexane-1-carbonyl-CoA [corrected].",Aug 1998,"D Laempe, W Eisenreich, A Bacher, G Fuchs"
+1050,98LIA/QU,,10.1007/BF02883019,,-,-,-,-,-,-,-,-
+1051,98LIA/WAN,,10.1016/S0040-6031(98)00464-X,,-,-,-,-,-,-,-,-
+1052,98LOV/LAU,9799130.0,10.1046/j.1432-1327.1998.2570286.x,,['eng'],257,1,286-90,European journal of biochemistry,"In principle, all biochemical reactions are reversible, though some are more reversible than others. The classical ribonuclease mechanism involves a reversible transphosphorylation step, followed by quasi irreversible hydrolysis of the cyclic intermediate. We performed isotope-exchange and intermediate-trapping experiments showing that the second hydrolysis step is readily reversible in the presence of RNase A or RNase T1. As a consequence, the equilibrium between a phosphodiester and a 2',3'-cyclophosphate accounts for all catalysed reactions, even if the leaving/attacking group is a water molecule. Therefore, ribonucleases are transferases rather than hydrolases. The equilibrium constant for the catalysed interconversion is close to 1 M. From this result, we estimate the effective concentration of the 2'-hydroxyl nucleophile in the cyclization step to be 10(7) M. The high effective concentration of the vicinal hydroxyl group balances the strain-associated and solvation-associated instability of the pentacyclic phosphodiester.",Oct 1998,"S Loverix, G Laus, J C Martins, L Wyns, J Steyaert"
+1053,98TEW,,10.1021/je980021x,,-,-,-,-,-,-,-,-
+1054,98TEW/CHE,,10.1021/jp982754u,,-,-,-,-,-,-,-,-
+1055,98TEW/KIS,,10.1006/jcht.1998.0342,,-,-,-,-,-,-,-,-
+1056,98THO/JOR,9466792.0,10.1006/abio.1997.2490,,['eng'],256,1,7-13,Analytical biochemistry,"We describe a multiwavelength method for measuring an enzyme's discrimination of one substrate over another by continuously monitoring the reactions of the two substrates simultaneously. This method is generally applicable to ultraviolet-visible diode array or rapid-scanning spectrophotometers and the measurement requires a single incubation of enzyme with two substrates. Rates at each of the wavelengths may be fit globally by using a nonlinear least-squares fitting procedure which provides adequate statistical analysis. The specificity of trypsin for N-alpha-benzoyl-L-arginine p-nitroanilide (BRpNA) over N-t-butyloxycarbonyl-L-alanine-p-nitrophenylester (BocApNP) was 2.1 as measured by the multiwavelength partition method and 2.3 by comparing the individual kcat/K(m)'s for the two substrates. Multiwavelength analysis was applied to two enzymes in the biosynthetic pathway for fungal melanin: scytalone dehydratase and trihydroxynaphthalene reductase from Magnaporthea grisea. The specificity of trihydroxynaphthalene reductase for 2,3-dihydro-2,5-dihydroxy-4H-benzopyran-4-one compared to scytalone, a natural substrate for the enzyme, was 95. Scytalone dehydratase was eight-fold more specific for 2,3-dihydro-2,5-dihydroxy-4H-benzopyran-4-one than it was for scytalone. Multiwavelength analysis was also used to measure an equilibrium constant of 0.040 for the reaction ¿dihydroorotate + oxonic acid<-->orotate + dihydrooxonic acid¿ catalyzed by dihydroorotate dehydrogenase. Advantages, limitations, and further applications of this steady-state method, which directly measures relative substrate specificities, are delineated. All studies described in this paper were at pH 7.0 and 25 degrees C.",Feb 1998,"J E Thompson, D B Jordan"
+1057,98URB/BRA,9922170.0,10.1021/bi981819g,,['eng'],37,51,18018-25,Biochemistry,"3-Fluorooxalacetate is a substrate for malic dehydrogenase. When enzymatic reduction is slower than the rate of epimerization of the two enantiomers, only (2R,3R)-erythro-fluoromalate is formed. Conversely, when a high enzyme level and excess of NADH lead to reduction that is fast relative to the epimerization rate, equal amounts of (2R,3R)-erythro- and (2R,3S)-threo-fluoromalate are formed. These data suggest that the V/K value for reduction of the R enantiomer to give the erythro isomer is approximately 100 times greater than for reduction of the S enantiomer to give the threo isomer. The equilibrium constant for the oxidation of fluoromalate is an order of magnitude less favorable than for oxidation of malate, while the equilibrium deuterium isotope effect from deuteration at C-2 of the substrate is 1.09 for fluoromalate versus 1.18 for malate. These effects reflect the inductive effect of fluorine at the 3-position.",Dec 1998,"J L Urbauer, D E Bradshaw, W W Cleland"
+1058,99BAS/MAR,10637769.0,10.1080/152165499306630,,['eng'],48,5,525-9,IUBMB life,"As a step toward analyzing the serine biosynthetic pathway in mammals, we have studied the properties of phosphoserine aminotransferase, the second step-catalyzing enzyme. The K(m) values for 3-phosphohydroxypyruvate and L-phosphoserine are 5 and 35 microM, respectively, and those for glutamate and alpha-ketoglutarate are 1.2 and 0.8 mM, respectively. The product inhibition studies strengthened the support for a ping-pong mechanism and allowed evaluation of Ki values for the four substrates. The equilibrium constant evaluated from the kinetic parameters is approximately 40. Additionally, some physical properties relative to the bound coenzyme and the secondary structure were investigated. The results are consistent with a structural relationship between the Escherichia coli enzyme and the mammalian enzyme. The mammalian enzyme has specific kinetic parameters, the determination of which is a prerequisite to analyzing the serine biosynthetic pathway in mammals.",Nov 1999,"M J Basurko, M Marche, M Darriet, A Cassaigne"
+1059,99BRA/FIS,10358012.0,10.1074/jbc.274.24.16727,,['eng'],274,24,16727-35,The Journal of biological chemistry,"GTP cyclohydrolase I catalyzes the conversion of GTP to dihydroneopterin triphosphate. The replacement of histidine 179 by other amino acids affords mutant enzymes that do not catalyze the formation of dihydroneopterin triphosphate. However, some of these mutant proteins catalyze the conversion of GTP to 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone 5'-triphosphate as shown by multinuclear NMR analysis. The equilibrium constant for the reversible conversion of GTP to the ring-opened derivative is approximately 0.1. The wild-type enzyme converts the formylamino pyrimidine derivative to dihydroneopterin triphosphate; the rate is similar to that observed with GTP as substrate. The data support the conclusion that the formylamino pyrimidine derivative is an intermediate in the overall reaction catalyzed by GTP cyclohydrolase I.",Jun 1999,"A Bracher, M Fischer, W Eisenreich, H Ritz, N Schramek, P Boyle, P Gentili, R Huber, H Nar, G Auerbach, A Bacher"
+1060,99ELS,,,,-,-,-,-,-,-,-,-
+1061,99GRA/NID,10455186.0,10.1074/jbc.274.35.25069,,['eng'],274,35,25069-77,The Journal of biological chemistry,"The thymidine diphosphate-L-rhamnose biosynthesis pathway is required for assembly of surface glycoconjugates in a growing list of bacterial pathogens, making this pathway a potential therapeutic target. However, the terminal reactions have not been characterized. To complete assignment of the reactions, the four enzymes (RmlABCD) that constitute the pathway in Salmonella enterica serovar Typhimurium LT2 were overexpressed. The purified RmlC and D enzymes together catalyze the terminal two steps involving NAD(P)H-dependent formation of dTDP-L-rhamnose from dTDP-6-deoxy-D-xylo-4-hexulose. RmlC was assigned as the thymidine diphosphate-4-dehydrorhamnose 3,5-epimerase by showing its activity to be NAD(P)H-independent. Spectrofluorometric and radiolabeling experiments were used to demonstrate the ability of RmlC to catalyze the formation of dTDP-6-deoxy-L-lyxo-4-hexulose from dTDP-6-deoxy-D-xylo-4-hexulose. Under reaction conditions, RmlC converted approximately 3% of its substrate to product. RmlD was unequivocally identified as the thymidine diphosphate-4-dehydrorhamnose reductase. The reductase property of RmlD was shown by equilibrium analysis and its ability to enable efficient biosynthesis of dTDP-L-rhamnose, even in the presence of low amounts of dTDP-6-deoxy-L-lyxo-4-hexulose. Comparison of 23 known and predicted RmlD sequences identified several conserved amino acid residues, especially the serine-tyrosine-lysine catalytic triad, characteristic for members of the reductase/epimerase/dehydrogenase protein superfamily. In conclusion, RmlD is a novel member of this protein superfamily.",Aug 1999,"M Graninger, B Nidetzky, D E Heinrichs, C Whitfield, P Messner"
+1062,99HUT/OEH,,10.1016/S0040-6031(98)00547-4,,-,-,-,-,-,-,-,-
+1063,99KAT/UED,10521704.0,10.1016/S1388-1981(99)00124-9,,['eng'],1440,2-3,205-14,Biochimica et biophysica acta,"Anandamide, an endogenous ligand for cannabinoid receptors, loses its biological activities when it is hydrolyzed to arachidonic acid and ethanolamine by anandamide amidohydrolase. We overexpressed a recombinant rat enzyme with a hexahistidine tag in a baculovirus-insect cell expression system, and purified the enzyme with the aid of a Ni-charged resin to a specific activity as high as 5.7 micromol/min/mg protein. The purified recombinant enzyme catalyzed not only the hydrolysis of anandamide and palmitoylethanolamide, but also their reverse synthetic reactions. In order to attain an equilibrium of the anandamide hydrolysis and its reverse reaction within 10 min, we utilized a large amount of the purified enzyme. The equilibrium constant ([arachidonic acid][ethanolamine])/([anandamide][water]) was calculated as 4x10(-3) (37 degrees C, pH 9.0). These experimental results with a purified enzyme preparation quantitatively confirmed the reversibility of the enzyme reaction previously observed with crude enzyme preparations.",Sep 1999,"K Katayama, N Ueda, I Katoh, S Yamamoto"
+1064,99KIS/HOL,,10.1006/jcht.1998.0444,,-,-,-,-,-,-,-,-
+1065,99KIS/TEW,,10.1006/jcht.1999.0496,,-,-,-,-,-,-,-,-
+1066,99MUN/LOP,10027985.0,10.1046/j.1365-2958.1999.01211.x,,['eng'],31,2,703-13,Molecular microbiology,"Uridine diphosphate galacturonate 4-epimerases (UDPGLEs) are enzymes that convert UDP-glucuronate into UDP-galacturonate. Although the presence of UDPGLEs has been reported in prokaryoic and eukaryotic organisms, the genes coding for these enzymes are completely unknown. The galacturonic acid-containing capsular polysaccharide of Streptococcus pneumoniae type 1 is synthesized through the action of a specific UDPGLE. We have constructed a defined deletion mutant in the cap1J gene (one of the 15 cap1 genes responsible for the synthesis of the type 1 capsule) that exhibited an unencapsulated phenotype. This mutant was unable to synthesize UDPGLE, suggesting that Cap1J was the type 1-specific UDPGLE of S. pneumoniae. Escherichia coli cells harbouring the recombinant plasmid pRMM38 (cap1J) overproduced a 40 kDa protein, characterized as Cap1J on the basis of the N-terminal amino acid sequence analysis, and expressed high levels of enzymatically active Cap1J epimerase. Cap1J was partially purified, although purification to electrophoretic homogeneity inactivated the enzyme irreversibly. The enzyme has the following characteristics: K(m) for UDP-glucuronate, 0.24 mM; pH optimum, 7.5; equilibrium constant (in the direction of UDP-galacturonate formation), 1.3; and an approximate M(r) of 80,000 for the active form. The Cap1J protein exhibited a fluorescence emission spectrum similar to that of NADH. Upon inactivation with p-hydroxymercuribenzoate, the addition of NAD+ and 2-mercaptoethanol were sufficient to reactivate the enzyme. Among several compounds tested, UDP-galactose and UDP-xylose exhibited the highest inhibition of the UDPGLE activity. Inactivation of UDPGLE activity was also observed in the presence of UMP and several reducing sugars. To our knowledge, this is the first example of a thoroughly molecular characterization of a UDPGLE.",Jan 1999,"R Muñoz, R López, M de Frutos, E García"
+1067,99NIE/SCH,,10.3109/10242429909040115,,-,-,-,-,-,-,-,-
+1068,99SAK/UTS,10087174.0,10.1006/abbi.1999.1121,,['eng'],364,1,125-8,Archives of biochemistry and biophysics,-,Apr 1999,"H Sakuraba, E Utsumi, C Kujo, T Ohshima"
+1069,99TEA/DOB,10428820.0,10.1074/jbc.274.32.22459,,['eng'],274,32,22459-63,The Journal of biological chemistry,"The effect of temperature, pH, free [Mg(2+)], and ionic strength on the apparent equilibrium constant of arginine kinase (EC 2.7.3.3) was determined. At equilibrium, the apparent K' was defined as [see text] where each reactant represents the sum of all the ionic and metal complex species. The K' at pH 7.0, 1.0 mM free [Mg(2+)], and 0. 25 M ionic strength was 29.91 +/- 0.59, 33.44 +/- 0.46, 35.44 +/- 0. 71, 39.64 +/- 0.74, and 45.19 +/- 0.65 (n = 8) at 40, 33, 25, 15, and 5 degrees C, respectively. The standard apparent enthalpy (DeltaH degrees') is -8.19 kJ mol(-1), and the corresponding standard apparent entropy of the reaction (DeltaS degrees') is + 2. 2 J K(-1)mol(-1) in the direction of ATP formation at pH 7.0, free [Mg(2+)] =1.0 mM, ionic strength (I) =0.25 M at 25 degrees C. We further show that the magnitude of transformed Gibbs energy (DeltaG degrees ') of -8.89 kJ mol(-1) is mostly comprised of the enthalpy of the reaction, with 7.4% coming from the entropy TDeltaS degrees' term (+0.66 kJ mol(-1)). Our results are discussed in relation to the thermodynamic properties of its evolutionary successor, creatine kinase.",Aug 1999,"W E Teague, G P Dobson"
+1070,99TEW/SCH,,10.1021/je980299p,,-,-,-,-,-,-,-,-
diff --git a/ruslan/DOI2META/task_18_prepare_a_pipeline_to_pull_data_about_publications.py b/ruslan/DOI2META/task_18_prepare_a_pipeline_to_pull_data_about_publications.py
new file mode 100644
index 0000000..bf4ee4b
--- /dev/null
+++ b/ruslan/DOI2META/task_18_prepare_a_pipeline_to_pull_data_about_publications.py
@@ -0,0 +1,179 @@
+# -*- coding: utf-8 -*-
+"""Task 18: prepare a pipeline to pull data about publications.ipynb
+
+Automatically generated by Colab.
+
+Original file is located at
+ https://colab.research.google.com/drive/1a_-pS-Qbb-J4m9Ykr5PnR7OFOsQla2b1
+"""
+
+pip install requests
+
+pip install biopython
+
+pip install odfpy
+
+!wget -O "openTECR recuration.ods" "https://docs.google.com/spreadsheets/d/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c/export?format=ods"
+
+import pandas as pd
+from Bio import Entrez
+import numpy as np
+import time
+
+def crossref(doi):
+ url = f"https://api.crossref.org/works/{doi}"
+ response = requests.get(url)
+ if response.status_code == 200:
+ return response.json()
+ else:
+ return {"error": f"DOI not found in CrossRef: {doi}"}
+
+def pubmed(pmid):
+ handle = Entrez.efetch(db="pubmed", id=pmid, retmode="xml")
+ response = Entrez.read(handle)
+ handle.close()
+ return response
+
+def doires2meta(response):
+ metadata = {}
+ metadata['Title'] = response['message']['title']
+ date = response['message']['created']['date-parts'][0]
+ metadata['Date'] = f'{date[2]}.{date[1]}.{date[0]}'
+ metadata['Publisher'] = response['message']['publisher']
+ metadata['License'] = response['message']['license'][0]['URL']
+ metadata['Type'] = response['message']['type']
+ metadata['Volume'] = response['message']['volume']
+ metadata['Issue'] = response['message']['issue']
+ metadata['Page'] = response['message']['page']
+ fn = []
+ sn = []
+ for b in response['message']['author']:
+ fn.append(b['given'])
+ sn.append(b['family'])
+
+ string = ''
+
+ for i in range(len(fn)):
+ string = string + fn[i] + " " + sn[i] + ", "
+
+ string = string[:-2]
+ metadata['Authors'] = string
+ metadata['Language'] = response['message']['language']
+ return metadata
+
+def pubmed2meta(response):
+ metadata = {}
+ try:
+ metadata['Language'] = response['PubmedArticle'][0]['MedlineCitation']['Article']['Language']
+ except:
+ metadata['Language'] = '-'
+ try:
+ metadata['Volume'] = response['PubmedArticle'][0]['MedlineCitation']['Article']['Journal']['JournalIssue']['Volume']
+ except:
+ metadata['Volume'] = '-'
+ try:
+ metadata['Issue'] = response['PubmedArticle'][0]['MedlineCitation']['Article']['Journal']['JournalIssue']['Issue']
+ except:
+ metadata['Issue'] = "-"
+ try:
+ metadata['Page'] = response['PubmedArticle'][0]['MedlineCitation']['Article']['Pagination']['MedlinePgn']
+ except:
+ metadata['Page'] = "-"
+ date = response['PubmedArticle'][0]['MedlineCitation']['Article']['Journal']['JournalIssue']['PubDate']
+ try:
+ metadata['Journal'] = response['PubmedArticle'][0]['MedlineCitation']['Article']['Journal']['Title']
+ except:
+ metadata['Journal'] = "-"
+ try:
+ metadata['Abstract'] = response['PubmedArticle'][0]['MedlineCitation']['Article']['Abstract']['AbstractText'][0]
+ except:
+ metadata['Abstract'] = '-'
+ #print(date)
+ try:
+ month = date['Month']
+ except:
+ month = ' '
+ year = date['Year']
+ metadata['Date'] = f'{month} {year}'
+ try:
+ fn = []
+ sn = []
+ for b in response['PubmedArticle'][0]['MedlineCitation']['Article']['AuthorList']:
+ fn.append(b['ForeName'])
+ sn.append(b['LastName'])
+
+ string = ''
+
+ for i in range(len(fn)):
+ string = string + fn[i] + " " + sn[i] + ", "
+
+ string = string[:-2]
+ metadata['Authors'] = string
+ except:
+ metadata['Authors'] = "-"
+ return metadata
+
+def return_blank(indi):
+ metadata = {}
+ if indi == "pub":
+ metadata['Language'] = '-'
+ metadata['Volume'] = '-'
+ metadata['Issue'] = '-'
+ metadata['Page'] = '-'
+ metadata['Journal'] = '-'
+ metadata['Abstract'] = '-'
+ metadata['Date'] = '-'
+ metadata['Authors'] = '-'
+ if indi == "doi":
+ metadata['Title'] = '-'
+ metadata['Language'] = '-'
+ metadata['Volume'] = '-'
+ metadata['Issue'] = '-'
+ metadata['Page'] = '-'
+ metadata['Publisher'] = '-'
+ metadata['Date'] = '-'
+ metadata['Authors'] = '-'
+ metadata['License'] = '-'
+ metadata['Type'] = '-'
+ return metadata
+
+Entrez.email = "ruslanibragimovut@outlook.com"
+df = pd.read_excel("openTECR recuration.ods", sheet_name="references")
+pmids = df['pmid'].to_list()
+dois = df['doi'].to_list()
+
+doismeta = []
+for d in dois:
+ if type(d) == type('Is a string?'):
+ r = crossref(d)
+ #print(r)
+
+ try:
+ d = doires2meta(r)
+ except:
+ d = return_blank('doi')
+
+ doismeta.append(d)
+ else:
+ c = return_blank('doi')
+ doismeta.append(c)
+
+pmidsmeta = []
+for pmid in pmids:
+ if np.isnan(pmid) == False:
+ time.sleep(1)
+ r = pubmed(str(pmid))
+ #print(r)
+ d = pubmed2meta(r)
+ pmidsmeta.append(d)
+ else:
+ c = return_blank('pub')
+ pmidsmeta.append(c)
+
+dfpub = pd.DataFrame(pmidsmeta)
+dfdoi = pd.DataFrame(doismeta)
+
+dfpubC = pd.concat([df, dfpub], axis=1)
+dfdoiC = pd.concat([df, dfdoi], axis=1)
+dfpubC.to_csv('openTECRmetadataPubMed.csv')
+dfdoiC.to_csv('openTECRmetadataDOI.csv')
\ No newline at end of file
diff --git a/ruslan/QC Script/Curation manual - Automated Quality Control.pdf b/ruslan/QC Script/Curation manual - Automated Quality Control.pdf
new file mode 100644
index 0000000..f709013
Binary files /dev/null and b/ruslan/QC Script/Curation manual - Automated Quality Control.pdf differ
diff --git a/ruslan/QC Script/QCscript.py b/ruslan/QC Script/QCscript.py
new file mode 100644
index 0000000..49ead10
--- /dev/null
+++ b/ruslan/QC Script/QCscript.py
@@ -0,0 +1,471 @@
+# -*- coding: utf-8 -*-
+"""Task 16: reproduce and publish the TECRDB QC script.ipynb
+
+Automatically generated by Colab.
+
+Original file is located at
+ https://colab.research.google.com/drive/14ibCmUjaxIcAkB1vh6tDLf8V8PUIxt3B
+"""
+
+!wget -O "openTECR recuration - actual data.csv" "https://docs.google.com/spreadsheets/d/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c/export?format=csv&gid=2123069643"
+!wget -O "openTECR recuration - table codes.csv" "https://docs.google.com/spreadsheets/d/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c/export?format=csv&gid=831893235"
+!wget -O "openTECR recuration - table metadata.csv" "https://docs.google.com/spreadsheets/d/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c/export?format=csv&gid=1475422539"
+!wget -O "openTECR recuration.ods" "https://docs.google.com/spreadsheets/d/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c/export?format=ods"
+!wget -O "TECRDB.csv" "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv"
+##Downloading openTECR and Noor data
+
+!pip install odfpy
+## Installing library for processing .ods file
+
+import pandas
+
+READ_CSV = True
+
+
+## data upload
+if READ_CSV:
+ df = pandas.read_csv("openTECR recuration - actual data.csv")
+else:
+ df = pandas.read_excel("openTECR recuration.ods", sheet_name="actual data")
+df = df.replace({"col l/r": {"l":1,"r":2}}) ##replaced l and r in col l/r with 1 and 2
+
+## containing NaNs
+print("containing NaNs:")
+
+#script that counts rows containing NaN values
+subset = ["part", "page", "col l/r", "table from top", "entry nr"]
+counter = df[subset].isna().any(axis=1).sum()
+print(f"A total of {counter} rows contained NaNs.")
+
+## QC
+
+## Checking for duplicates
+## Replaced reference with reference_code as it is the real column name
+## Not actually needed anymore due ot duplicable table column
+
+if True:
+ ## duplicates and errors
+ test_df = df
+ MANUALLY_EXCLUDED_DUPLICATES = [
+ "54STA",
+ "71TAN/JOH",
+ "91HOR/UEH",
+ "76SCH/KRI",
+ "99TEW/SCH"
+ ]
+ ## shouldn't be necessary after introduction of duplicate_table column; so we use:
+ MANUALLY_EXCLUDED_DUPLICATES = []
+ ##
+ test_df = test_df[~test_df.reference_code.isin(MANUALLY_EXCLUDED_DUPLICATES)]
+ assert sum(test_df[((test_df["entry nr"]=="duplicate") | (test_df["entry nr"]=="error"))].id.isna())==0, ("Duplicate or error found for an empty-ID row", test_df[(((test_df["entry nr"]=="duplicate") | (test_df["entry nr"]=="error"))) & test_df.id.isna()])
+ ## Ensures that rows containing duplicate or error in entry nr column also has an appropriate ID.
+
+#print("I am removing the following duplicates and errors:")
+df = df[~((df["entry nr"]=="duplicate") | (df["entry nr"]=="error"))]
+## Removes such rows
+
+#QC
+if True:
+ ##check completeness of position annotation
+ na_counter = df[["part","page","col l/r","table from top", "entry nr"]].isna().sum(axis="columns") ##Counts NaN values in position annotation
+ #print(na_counter)
+ assert len(df[~na_counter.isin([0,5])])==0, print(df[~na_counter.isin([0,5])][["id","reference","part","page","col l/r","table from top", "entry nr"]].to_string())
+ #Prints problematic rows if any
+
+ ##Checks for spaces in /reference_code/ column.
+ assert len(df[df.reference_code.str.contains(" ").fillna(False)])==0, print(df[df.reference_code.str.contains(" ").fillna(False)].to_string())
+ ## And output problematic rows.
+
+## drop NaNs -- these entries just haven't been worked on and can't be checked
+df = df.dropna(subset=["part","page","col l/r","table from top", "entry nr"])
+
+## convert values in columns part, page, col l/r, table from top and entry nr to integers
+df[["part","page","col l/r","table from top", "entry nr"]] = df[["part","page","col l/r","table from top", "entry nr"]].astype(int)
+
+## quality check new data
+
+if True:
+ ## id is unique
+ assert len(df.dropna(subset=["id"]).id.unique()) == len(df.dropna(subset=["id"])), df.dropna(subset=["id"])[df.dropna(subset=["id"]).id.duplicated()].to_string()
+ ## Ensures that every value in column ID is unique, if not prints out problematic tows.
+
+ ## tables intact in themselves
+
+ ##Groups rows in dataframe by part, page, col l/r, and table from top values.
+
+ for which, g in df.groupby(["part","page","col l/r","table from top"]): # g is subset corresponding to specific part of the dataframe, as grouped by previously
+ #print((which,g))
+ #if which == (3, 1091, 1, 1):
+ # continue
+
+ assert len(g.reference_code.unique())==1, (which, print(g.to_string())) ## Checks that all values in reference_code have the same value--
+ assert len(g.EC.unique()) == 1, (which, print(g.to_string())) ## Check that all EC values are uniform
+ assert len(g.reaction.unique())==1, (which, print(g.to_string())) ## - fixed "description" for correct column name
+ assert sorted(g["entry nr"].values)==list(range(1,g["entry nr"].max()+1)), (which, print(g.to_string())) ## Check that all values in entry nr are ordered from lowest to highest
+
+ ## table counts consistently continuous
+ for which, g in df.groupby(["part", "page", "col l/r"]):
+ ## the following part/page/column combinations
+ #
+ # contain a table which was mentioned before;
+ ## the table is thus marked full duplicate and was removed beforehand; so we manually
+ ## exclude those from this automated check
+ MANUALLY_EXCLUDED_COLUMNS = [
+ (2, 558, 2),
+ (2, 560, 2),
+ (2, 566, 2),
+ (2, 584, 1),
+ (2, 590, 2),
+ (3, 1041, 1),
+ (3, 1076, 2),
+ (7, 1360, 2),
+ (7, 1369, 2),
+ (7, 1373, 1),
+ ]
+ ## shouldn't be necessary after introduction of duplicate_table column; so we use:
+ MANUALLY_EXCLUDED_COLUMNS = []
+ ## because there is a peculiarity about tables not-existent-in-the-pdf, but found in randr, we have to use:
+ MANUALLY_EXCLUDED_COLUMNS = [
+ (6, 948, 2),
+ (6, 949, 1),
+ ]
+ if which in MANUALLY_EXCLUDED_COLUMNS:
+ continue
+ assert sorted(g["table from top"].unique()) == list(range(1, g["table from top"].max() + 1)), (which, print(g.to_string())) # ensures that values in table from top are from lowest to highest
+
+ ## column values either 1 or 2
+ for which, g in df.groupby(["part", "page"]):
+ assert all([i in [1,2] for i in g["col l/r"].values]), (which, print(g.to_string())) # ensures that all values in col l/r are either 1 or 2
+
+ ## page numbers consistently continuous
+ for which, g in df.groupby("part"):
+ MANUALLY_EXCLUDED_PARTS = [
+ #2,
+ #3,
+ #7
+ ]
+ if which in MANUALLY_EXCLUDED_PARTS: #ensures that page numbers are continious by parts
+ continue
+
+ print(f"----- This is about part {which} -----")
+ should_be = list(range(g["page"].min(), g["page"].max() + 1))
+ for page in should_be:
+ if page not in g["page"].unique():
+ print(f"Missing page: {page}") #Finds missing pages and prints them out
+ #assert sorted(g["page"].unique()) == list(range(g["page"].min(), g["page"].max() + 1))
+
+## extract added values
+# print(f"You will need to care for these {df.id.isna().sum()} recently added rows:")
+# print(df[df.id.isna()])
+
+print("The online spreadsheet data looks consistent.")
+
+## consistency check between online spreadsheet and original Noor data
+##Reading TECRDB and openTECR files
+noor = pandas.read_csv("TECRDB.csv")
+noor = noor.rename(columns={"reaction": "keggID"})
+noor = noor.rename(columns={"reference": "reference_code",'description':'reaction'})
+## Updating column names in Noor set to match the new columns in openTECR.
+if READ_CSV:
+ online = pandas.read_csv("openTECR recuration - actual data.csv")
+else:
+ online = pandas.read_excel("openTECR recuration.ods", sheet_name="actual data")
+
+
+online = online.replace({"col l/r": {"l":1,"r":2}}) #replacing l/r values with 1 and 2
+## check that all ids are still there
+assert set(noor.id) - set(online.id) == set(), f"The following IDs were deleted online: {set(noor.id)-set(online.id)}"
+## Checks that all ID are present in both openTECR and Noor
+
+## non-curated values should not have been changed by anyone!
+leftjoined = pandas.merge(noor, online.dropna(subset="id"), on="id", how="left", validate="1:1")
+## Merging noor set and openTECR together
+
+## This code snippet tries to check if K_prime values are equal in Noor and openTECR dataset
+## While accounting for rounding up in openTECR
+## If values are not equal despite being rounded up, it will output both k_prime values from noor and openTECR
+## kPn is a prime_K column from Noor set roughly rounded up by the rules outlined in openTECR
+
+
+
+import numpy as np
+kPn = []
+for i in range(len(leftjoined.K_prime_x)):
+ if leftjoined.K_prime_x[i] != leftjoined.K_prime_y[i]:
+ if np.isnan(leftjoined.K_prime_x[i]) == False:
+ #print(leftjoined.K_prime_x[i])
+ #print(leftjoined.K_prime_y[i])
+ ##Trying to match weird rounding up format of openTECR Kprime values
+ if len(str(leftjoined.K_prime_x[i]).split('.')[1])>4:
+ rounded = round(leftjoined.K_prime_x[i],len(str(leftjoined.K_prime_x[i]).split('.')[1])-1)
+ #print(rounded)
+ elif len(str(leftjoined.K_prime_x[i]).split('.')[1])==2:
+ rounded = round(leftjoined.K_prime_x[i],1)
+ #print(rounded)
+ elif len(str(leftjoined.K_prime_x[i]).split('.')[1])==3:
+ rounded = round(leftjoined.K_prime_x[i], 2)
+ #print(rounded)
+ elif len(str(leftjoined.K_prime_x[i]).split('.')[1])==1:
+ rounded = round(leftjoined.K_prime_x[i], 0)
+ #print(rounded)
+ #print(round(leftjoined.K_prime_x[i], 2))
+ if rounded+0.1 == leftjoined.K_prime_y[i]:
+ kPn.append(rounded+0.1)
+ else:
+ kPn.append(rounded)
+ else:
+ kPn.append(leftjoined.K_prime_x[i])
+ else:
+ kPn.append(leftjoined.K_prime_x[i])
+for i in range(len(leftjoined.K_prime_y)):
+ if kPn[i] != leftjoined.K_prime_y[i]:
+ if np.isnan(leftjoined.K_prime_y[i]) == False:
+ print(f'Noor set K_prime value: {kPn[i]}')
+ print(f'openTECR set K_prime value: {leftjoined.K_prime_y[i]}')
+## Some cases couldn't be handled since they don't follow rounding logic
+
+## Columns that should be the same
+SHOULD_BE_THE_SAME = [
+ "reference_code",
+ "EC",
+ "reaction",
+ "K",
+ "temperature",
+ "ionic_strength",
+ "p_h",
+ "p_mg",
+ #"K_prime", # - checked manually, weird rounding up in online data? Handled by code above
+]
+for s in SHOULD_BE_THE_SAME:
+ entries_where_both_are_nans = leftjoined[ leftjoined[f"{s}_x"].isna() & leftjoined[f"{s}_y"].isna() ]
+ if len(entries_where_both_are_nans) == 0:
+ assert (leftjoined[f"{s}_x"] == leftjoined[f"{s}_y"]).all(), (s, print(leftjoined[~(leftjoined[f"{s}_x"] == leftjoined[f"{s}_y"])][["id",f"{s}_x",f"{s}_y"]].to_string()))
+ else:
+ tmp = leftjoined[ ~ (leftjoined[f"{s}_x"].isna() & leftjoined[f"{s}_y"].isna()) ]
+ assert (tmp[f"{s}_x"] == tmp[f"{s}_y"]).all(), (s, print(tmp[~(tmp[f"{s}_x"] == tmp[f"{s}_y"])][["id",f"{s}_x",f"{s}_y"]].to_string()))
+
+## The code above checks that all values in those columns between both Noor (_x) and openTECR (_y) are either NaN or equal. If not, raises assertion error and prints out incorrect rows
+
+## did someone add a new row without id, where they should have corrected a row with id?
+merged = pandas.merge(online, noor, on=[
+ "reference_code",
+ "temperature",
+ "ionic_strength",
+ "p_h",
+ "p_mg",
+ "K_prime",
+])
+merged = merged[merged["id_x"] != merged["id_y"]]
+potential_errors = merged[merged["id_x"].isna() | merged["id_y"].isna()]
+
+## Checks whether or not noor and online set have matching ID values
+
+## the following have been manually checked to be able to be excluded from the comparison below:
+MANUALLY_EXCLUDED = [
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4356",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1714",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1715",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1716",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1718",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1717",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2140",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2149",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3167",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3184",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry707",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4246",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry392",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1269",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4283",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4284",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3888",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3896",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3897",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1915",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1603",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1605",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry236",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry386",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2718",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3560",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3561",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4006",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1271",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1586",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1589",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1590",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1591",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1588",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1587",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2370",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2371",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1601",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3637",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2725",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry705",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry702",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry704",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4040",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4373",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1829",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3031",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3032",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2339",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1916",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3026",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4086",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2848",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4316",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry772",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2851",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry398",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry82",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry806",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry805",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3654",
+ "https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2277",
+]
+potential_errors = potential_errors[ ~potential_errors.id_y.isin(MANUALLY_EXCLUDED) ]
+if len(potential_errors) > 0:
+ print("The following entries might have been added as a new row without id, where they should have corrected a row with id:")
+ print(potential_errors.to_string())
+
+print("The online spreadsheet data and its original data source are still in sync.")
+
+## annotate online spreadsheet with table_codes
+#
+#
+## read second df
+## -- get it manually from https://zenodo.org/record/5495826 !
+noor = pandas.read_csv("TECRDB.csv")
+noor.columns
+#Index(['id', 'url', 'reference', 'method', 'eval', 'EC', 'enzyme_name',
+# 'reaction', 'description', 'K', 'K_prime', 'temperature',
+# 'ionic_strength', 'p_h', 'p_mg'],
+
+noor = noor.drop(['K', 'K_prime', 'temperature',
+ 'ionic_strength', 'p_h', 'p_mg'],axis="columns")
+
+## Fixed to matching name in openTECR
+noor = noor.rename(columns={"reaction": "keggID"})
+noor = noor.rename(columns={"reference": "reference_code",'description':'reaction'})
+
+## extract table codes
+noor["table_code"] = noor.url.str.split("&T1=").str[-1]
+
+## quality check
+if True:
+ ## tables intact in themselves
+ for which, g in noor.groupby("table_code"):
+ #print((which,g))
+ assert len(g.reference_code.unique())==1, (which, print(g.to_string()))
+ assert len(g.method.unique())==1, (which, print(g.to_string()))
+ assert len(g["eval"].unique()) == 1, (which, print(g.to_string()))
+ assert len(g.EC.unique()) == 1, (which, print(g.to_string()))
+ assert len(g.enzyme_name.unique())==1, (which, print(g.to_string()))
+ assert len(g.reaction.unique()) == 1, (which, print(g.to_string()))
+ assert len(g.reaction.unique()) == 1, (which, print(g.to_string()))
+
+## Ensures that all values in those columns are consistent
+
+## drop now-unnecessary columns
+noor = noor.drop(["EC","reference_code", "reaction"], axis="columns")
+#df = df.drop( ["description"], axis="columns")
+
+## merge
+tmp = pandas.merge(df, noor, how="left", on="id")
+
+## add manually extracted table codes
+if READ_CSV:
+ manual_table_codes = pandas.read_csv("openTECR recuration - table codes.csv")
+else:
+ manual_table_codes = pandas.read_excel("openTECR recuration.ods", sheet_name="manually mapped table codes")
+
+# QC
+if True:
+ assert sum(manual_table_codes.duplicated(["part", "page", "col l/r", "table from top"])) == 0, print(
+ manual_table_codes[manual_table_codes.duplicated(["part", "page", "col l/r", "table from top"])])
+# split into tables with table codes from Noor and those which needed to be annotated manually
+manual_table_codes = manual_table_codes.drop(["reference", "description"], axis="columns")
+tmp_with_table_codes = tmp[~tmp.table_code.isna()]
+tmp_without_table_codes = tmp[tmp.table_code.isna()]
+tmp_without_table_codes = tmp_without_table_codes.drop("table_code", axis="columns")
+tmp_without_table_codes_try_to_add_manual_ones = pandas.merge(tmp_without_table_codes, manual_table_codes, how="left", on=["part","page","col l/r","table from top"])
+# concat the two
+new = pandas.concat([tmp_with_table_codes, tmp_without_table_codes_try_to_add_manual_ones], ignore_index=True)
+## keep only one entry per table code, remove now-meaningless columns, but keep id=NaN rows
+new = new[~new.duplicated(["part","page","col l/r","table from top"])]
+new = new.drop(["id","url"], axis="columns")
+new["comment"] = ""
+
+## Ensures no diplicate values in manual_table_codes
+## Splits tmp into portitions with and without table_codes
+## Removes duplicate entries and adds column "comment" for further annotation
+
+## export tables which need to be added to the "table codes" tab
+selector = []
+for i,s in new.iterrows():
+ if pandas.isna(s.table_code):
+ if len(manual_table_codes[(manual_table_codes.part == s.part) &
+ (manual_table_codes.page == s.page) &
+ (manual_table_codes["col l/r"] == s["col l/r"]) &
+ (manual_table_codes["table from top"] == s["table from top"])
+ ]) == 0:
+ selector.append(i)
+export = new.loc[selector]
+(export[[
+ "part","page","col l/r","table from top",
+ "table_code",
+ "reaction",
+ "reference_code",
+ "curator",
+ ]]
+ .sort_values(["part","page","col l/r","table from top"])
+ .to_csv("2024-01-06-opentecr-recuration.missing_table_codes.csv", index=False)
+ )
+
+## identifies and exports rows from the new DataFrame that are missing table_code values and do not already exist in manual_table_codes, creating a CSV file with them
+## selector - rows that need to be exported
+
+
+## export tables which need to have their comment extracted
+selector = []
+if READ_CSV:
+ tables_with_comments = pandas.read_csv("openTECR recuration - table metadata.csv")
+else:
+ tables_with_comments = pandas.read_excel("openTECR recuration.ods", sheet_name="table comments")
+## QC
+if True:
+ assert sum(tables_with_comments.duplicated(["part","page","col l/r","table from top"]))==0, print(tables_with_comments[tables_with_comments.duplicated(["part","page","col l/r","table from top"])])
+
+# Identify rows in new df that are not present in the metadata
+for i, s in new.iterrows():
+ # Check if a matching entry exists in `tables_with_comments`
+ if len(tables_with_comments[
+ (tables_with_comments.part == s.part) &
+ (tables_with_comments.page == s.page) &
+ (tables_with_comments["col l/r"] == s["col l/r"]) &
+ (tables_with_comments["table from top"] == s["table from top"])
+ ]) == 0:
+ # If no match is found, add the index of the row to `selector`
+ selector.append(i)
+
+tables_without_comments = new.loc[selector]
+# Add placeholders for manual annotation and spellchecking
+tables_without_comments["manually spellchecked"] = ""
+tables_without_comments["comment"] = ""
+
+
+# Export the filtered data to a CSV file
+
+(tables_without_comments[[
+ "part","page","col l/r","table from top",
+ "reference_code",
+ "manually spellchecked",
+ "comment"
+ ]]
+ .sort_values(["part","page","col l/r","table from top"])
+ .to_csv("2024-01-06-opentecr-recuration.missing-table-comments.csv", index=False)
+ )
+
+print("I could merge the online spreadsheet and the Noor data. I have written file regarding the tables to your disk.")
\ No newline at end of file
diff --git a/ruslan/QC Script/Task_16_reproduce_and_publish_the_TECRDB_QC_script.ipynb b/ruslan/QC Script/Task_16_reproduce_and_publish_the_TECRDB_QC_script.ipynb
new file mode 100644
index 0000000..74efa46
--- /dev/null
+++ b/ruslan/QC Script/Task_16_reproduce_and_publish_the_TECRDB_QC_script.ipynb
@@ -0,0 +1,754 @@
+{
+ "nbformat": 4,
+ "nbformat_minor": 0,
+ "metadata": {
+ "colab": {
+ "provenance": []
+ },
+ "kernelspec": {
+ "name": "python3",
+ "display_name": "Python 3"
+ },
+ "language_info": {
+ "name": "python"
+ }
+ },
+ "cells": [
+ {
+ "cell_type": "code",
+ "execution_count": null,
+ "metadata": {
+ "colab": {
+ "base_uri": "https://localhost:8080/"
+ },
+ "id": "YX8E1Mkij485",
+ "outputId": "09e80646-6518-420d-9cbb-9104ff7dff91"
+ },
+ "outputs": [
+ {
+ "output_type": "stream",
+ "name": "stdout",
+ "text": [
+ "--2025-01-17 18:59:21-- https://docs.google.com/spreadsheets/d/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c/export?format=csv&gid=2123069643\n",
+ "Resolving docs.google.com (docs.google.com)... 74.125.128.100, 74.125.128.113, 74.125.128.139, ...\n",
+ "Connecting to docs.google.com (docs.google.com)|74.125.128.100|:443... connected.\n",
+ "HTTP request sent, awaiting response... 307 Temporary Redirect\n",
+ "Location: https://doc-00-8k-sheets.googleusercontent.com/export/54bogvaave6cua4cdnls17ksc4/73nbh4anccgrg7oplu9esnjpjo/1737140360000/115120384215235060766/*/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c?format=csv&gid=2123069643 [following]\n",
+ "Warning: wildcards not supported in HTTP.\n",
+ "--2025-01-17 18:59:21-- https://doc-00-8k-sheets.googleusercontent.com/export/54bogvaave6cua4cdnls17ksc4/73nbh4anccgrg7oplu9esnjpjo/1737140360000/115120384215235060766/*/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c?format=csv&gid=2123069643\n",
+ "Resolving doc-00-8k-sheets.googleusercontent.com (doc-00-8k-sheets.googleusercontent.com)... 173.194.69.132, 2a00:1450:4013:c04::84\n",
+ "Connecting to doc-00-8k-sheets.googleusercontent.com (doc-00-8k-sheets.googleusercontent.com)|173.194.69.132|:443... connected.\n",
+ "HTTP request sent, awaiting response... 200 OK\n",
+ "Length: unspecified [text/csv]\n",
+ "Saving to: ‘openTECR recuration - actual data.csv’\n",
+ "\n",
+ "openTECR recuration [ <=> ] 1.22M --.-KB/s in 0.1s \n",
+ "\n",
+ "2025-01-17 18:59:22 (9.33 MB/s) - ‘openTECR recuration - actual data.csv’ saved [1276759]\n",
+ "\n",
+ "--2025-01-17 18:59:22-- https://docs.google.com/spreadsheets/d/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c/export?format=csv&gid=831893235\n",
+ "Resolving docs.google.com (docs.google.com)... 74.125.128.100, 74.125.128.113, 74.125.128.139, ...\n",
+ "Connecting to docs.google.com (docs.google.com)|74.125.128.100|:443... connected.\n",
+ "HTTP request sent, awaiting response... 307 Temporary Redirect\n",
+ "Location: https://doc-00-8k-sheets.googleusercontent.com/export/54bogvaave6cua4cdnls17ksc4/73nbh4anccgrg7oplu9esnjpjo/1737140360000/115120384215235060766/*/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c?format=csv&gid=831893235 [following]\n",
+ "Warning: wildcards not supported in HTTP.\n",
+ "--2025-01-17 18:59:22-- https://doc-00-8k-sheets.googleusercontent.com/export/54bogvaave6cua4cdnls17ksc4/73nbh4anccgrg7oplu9esnjpjo/1737140360000/115120384215235060766/*/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c?format=csv&gid=831893235\n",
+ "Resolving doc-00-8k-sheets.googleusercontent.com (doc-00-8k-sheets.googleusercontent.com)... 173.194.69.132, 2a00:1450:4013:c04::84\n",
+ "Connecting to doc-00-8k-sheets.googleusercontent.com (doc-00-8k-sheets.googleusercontent.com)|173.194.69.132|:443... connected.\n",
+ "HTTP request sent, awaiting response... 200 OK\n",
+ "Length: unspecified [text/csv]\n",
+ "Saving to: ‘openTECR recuration - table codes.csv’\n",
+ "\n",
+ "openTECR recuration [ <=> ] 48.61K --.-KB/s in 0.008s \n",
+ "\n",
+ "2025-01-17 18:59:23 (5.64 MB/s) - ‘openTECR recuration - table codes.csv’ saved [49780]\n",
+ "\n",
+ "--2025-01-17 18:59:23-- https://docs.google.com/spreadsheets/d/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c/export?format=csv&gid=1475422539\n",
+ "Resolving docs.google.com (docs.google.com)... 74.125.128.100, 74.125.128.113, 74.125.128.139, ...\n",
+ "Connecting to docs.google.com (docs.google.com)|74.125.128.100|:443... connected.\n",
+ "HTTP request sent, awaiting response... 307 Temporary Redirect\n",
+ "Location: https://doc-00-8k-sheets.googleusercontent.com/export/54bogvaave6cua4cdnls17ksc4/73nbh4anccgrg7oplu9esnjpjo/1737140360000/115120384215235060766/*/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c?format=csv&gid=1475422539 [following]\n",
+ "Warning: wildcards not supported in HTTP.\n",
+ "--2025-01-17 18:59:23-- https://doc-00-8k-sheets.googleusercontent.com/export/54bogvaave6cua4cdnls17ksc4/73nbh4anccgrg7oplu9esnjpjo/1737140360000/115120384215235060766/*/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c?format=csv&gid=1475422539\n",
+ "Resolving doc-00-8k-sheets.googleusercontent.com (doc-00-8k-sheets.googleusercontent.com)... 173.194.69.132, 2a00:1450:4013:c04::84\n",
+ "Connecting to doc-00-8k-sheets.googleusercontent.com (doc-00-8k-sheets.googleusercontent.com)|173.194.69.132|:443... connected.\n",
+ "HTTP request sent, awaiting response... 200 OK\n",
+ "Length: unspecified [text/csv]\n",
+ "Saving to: ‘openTECR recuration - table metadata.csv’\n",
+ "\n",
+ "openTECR recuration [ <=> ] 211.38K --.-KB/s in 0.04s \n",
+ "\n",
+ "2025-01-17 18:59:24 (5.36 MB/s) - ‘openTECR recuration - table metadata.csv’ saved [216452]\n",
+ "\n",
+ "--2025-01-17 18:59:24-- https://docs.google.com/spreadsheets/d/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c/export?format=ods\n",
+ "Resolving docs.google.com (docs.google.com)... 74.125.128.100, 74.125.128.113, 74.125.128.139, ...\n",
+ "Connecting to docs.google.com (docs.google.com)|74.125.128.100|:443... connected.\n",
+ "HTTP request sent, awaiting response... 307 Temporary Redirect\n",
+ "Location: https://doc-00-8k-sheets.googleusercontent.com/export/54bogvaave6cua4cdnls17ksc4/73nbh4anccgrg7oplu9esnjpjo/1737140360000/115120384215235060766/*/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c?format=ods [following]\n",
+ "Warning: wildcards not supported in HTTP.\n",
+ "--2025-01-17 18:59:24-- https://doc-00-8k-sheets.googleusercontent.com/export/54bogvaave6cua4cdnls17ksc4/73nbh4anccgrg7oplu9esnjpjo/1737140360000/115120384215235060766/*/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c?format=ods\n",
+ "Resolving doc-00-8k-sheets.googleusercontent.com (doc-00-8k-sheets.googleusercontent.com)... 173.194.69.132, 2a00:1450:4013:c04::84\n",
+ "Connecting to doc-00-8k-sheets.googleusercontent.com (doc-00-8k-sheets.googleusercontent.com)|173.194.69.132|:443... connected.\n",
+ "HTTP request sent, awaiting response... 200 OK\n",
+ "Length: unspecified [application/vnd.oasis.opendocument.spreadsheet]\n",
+ "Saving to: ‘openTECR recuration.ods’\n",
+ "\n",
+ "openTECR recuration [ <=> ] 2.43M 3.88MB/s in 0.6s \n",
+ "\n",
+ "2025-01-17 18:59:43 (3.88 MB/s) - ‘openTECR recuration.ods’ saved [2548477]\n",
+ "\n",
+ "--2025-01-17 18:59:43-- https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv\n",
+ "Resolving w3id.org (w3id.org)... 162.209.11.63, 2001:4801:7820:75:be76:4eff:fe10:16a2\n",
+ "Connecting to w3id.org (w3id.org)|162.209.11.63|:443... connected.\n",
+ "HTTP request sent, awaiting response... 303 See Other\n",
+ "Location: https://zenodo.org/record/5495826/files/TECRDB.csv [following]\n",
+ "--2025-01-17 18:59:44-- https://zenodo.org/record/5495826/files/TECRDB.csv\n",
+ "Resolving zenodo.org (zenodo.org)... 188.185.45.92, 188.185.48.194, 188.185.43.25, ...\n",
+ "Connecting to zenodo.org (zenodo.org)|188.185.45.92|:443... connected.\n",
+ "HTTP request sent, awaiting response... 301 MOVED PERMANENTLY\n",
+ "Location: /records/5495826/files/TECRDB.csv [following]\n",
+ "--2025-01-17 18:59:44-- https://zenodo.org/records/5495826/files/TECRDB.csv\n",
+ "Reusing existing connection to zenodo.org:443.\n",
+ "HTTP request sent, awaiting response... 200 OK\n",
+ "Length: 1662362 (1.6M) [text/plain]\n",
+ "Saving to: ‘TECRDB.csv’\n",
+ "\n",
+ "TECRDB.csv 100%[===================>] 1.58M 10.4MB/s in 0.2s \n",
+ "\n",
+ "2025-01-17 18:59:44 (10.4 MB/s) - ‘TECRDB.csv’ saved [1662362/1662362]\n",
+ "\n"
+ ]
+ }
+ ],
+ "source": [
+ "!wget -O \"openTECR recuration - actual data.csv\" \"https://docs.google.com/spreadsheets/d/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c/export?format=csv&gid=2123069643\"\n",
+ "!wget -O \"openTECR recuration - table codes.csv\" \"https://docs.google.com/spreadsheets/d/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c/export?format=csv&gid=831893235\"\n",
+ "!wget -O \"openTECR recuration - table metadata.csv\" \"https://docs.google.com/spreadsheets/d/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c/export?format=csv&gid=1475422539\"\n",
+ "!wget -O \"openTECR recuration.ods\" \"https://docs.google.com/spreadsheets/d/1jLIxEXVzE2SAzIB0UxBfcFoHrzjzf9euB6ART2VDE8c/export?format=ods\"\n",
+ "!wget -O \"TECRDB.csv\" \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv\"\n",
+ "##Downloading openTECR and Noor data"
+ ]
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "!pip install odfpy\n",
+ "## Installing library for processing .ods file"
+ ],
+ "metadata": {
+ "colab": {
+ "base_uri": "https://localhost:8080/"
+ },
+ "id": "Z3iv5JwRk1Sk",
+ "outputId": "b0d47e0f-45e2-4471-f921-a7e62a8575f2"
+ },
+ "execution_count": null,
+ "outputs": [
+ {
+ "output_type": "stream",
+ "name": "stdout",
+ "text": [
+ "Collecting odfpy\n",
+ " Downloading odfpy-1.4.1.tar.gz (717 kB)\n",
+ "\u001b[?25l \u001b[90m━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━\u001b[0m \u001b[32m0.0/717.0 kB\u001b[0m \u001b[31m?\u001b[0m eta \u001b[36m-:--:--\u001b[0m\r\u001b[2K \u001b[91m━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━\u001b[0m\u001b[91m╸\u001b[0m \u001b[32m716.8/717.0 kB\u001b[0m \u001b[31m33.1 MB/s\u001b[0m eta \u001b[36m0:00:01\u001b[0m\r\u001b[2K \u001b[90m━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━━\u001b[0m \u001b[32m717.0/717.0 kB\u001b[0m \u001b[31m18.4 MB/s\u001b[0m eta \u001b[36m0:00:00\u001b[0m\n",
+ "\u001b[?25h Preparing metadata (setup.py) ... \u001b[?25l\u001b[?25hdone\n",
+ "Requirement already satisfied: defusedxml in /usr/local/lib/python3.11/dist-packages (from odfpy) (0.7.1)\n",
+ "Building wheels for collected packages: odfpy\n",
+ " Building wheel for odfpy (setup.py) ... \u001b[?25l\u001b[?25hdone\n",
+ " Created wheel for odfpy: filename=odfpy-1.4.1-py2.py3-none-any.whl size=160672 sha256=21887d614af743c8b1238dc15d7e101e0de368e5d08284e9c144872a5f072e2a\n",
+ " Stored in directory: /root/.cache/pip/wheels/d6/1d/c8/8c29be1d73ca42d15977c75193d9f39a98499413c2838ac54c\n",
+ "Successfully built odfpy\n",
+ "Installing collected packages: odfpy\n",
+ "Successfully installed odfpy-1.4.1\n"
+ ]
+ }
+ ]
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "import pandas\n",
+ "\n",
+ "READ_CSV = True\n",
+ "\n",
+ "\n",
+ "## data upload\n",
+ "if READ_CSV:\n",
+ " df = pandas.read_csv(\"openTECR recuration - actual data.csv\")\n",
+ "else:\n",
+ " df = pandas.read_excel(\"openTECR recuration.ods\", sheet_name=\"actual data\")\n",
+ "df = df.replace({\"col l/r\": {\"l\":1,\"r\":2}}) ##replaced l and r in col l/r with 1 and 2\n",
+ "\n",
+ "## containing NaNs\n",
+ "print(\"containing NaNs:\")\n",
+ "\n",
+ "#script that counts rows containing NaN values\n",
+ "subset = [\"part\", \"page\", \"col l/r\", \"table from top\", \"entry nr\"]\n",
+ "counter = df[subset].isna().any(axis=1).sum()\n",
+ "print(f\"A total of {counter} rows contained NaNs.\")"
+ ],
+ "metadata": {
+ "colab": {
+ "base_uri": "https://localhost:8080/"
+ },
+ "id": "IcRQYEBSkLGV",
+ "outputId": "b59e61af-032b-4739-db03-02995db9589b"
+ },
+ "execution_count": null,
+ "outputs": [
+ {
+ "output_type": "stream",
+ "name": "stdout",
+ "text": [
+ "containing NaNs:\n",
+ "A total of 10 rows contained NaNs.\n"
+ ]
+ }
+ ]
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "## QC\n",
+ "\n",
+ "## Checking for duplicates\n",
+ "## Replaced reference with reference_code as it is the real column name\n",
+ "## Not actually needed anymore due ot duplicable table column\n",
+ "\n",
+ "if True:\n",
+ " ## duplicates and errors\n",
+ " test_df = df\n",
+ " MANUALLY_EXCLUDED_DUPLICATES = [\n",
+ " \"54STA\",\n",
+ " \"71TAN/JOH\",\n",
+ " \"91HOR/UEH\",\n",
+ " \"76SCH/KRI\",\n",
+ " \"99TEW/SCH\"\n",
+ " ]\n",
+ " ## shouldn't be necessary after introduction of duplicate_table column; so we use:\n",
+ " MANUALLY_EXCLUDED_DUPLICATES = []\n",
+ " ##\n",
+ " test_df = test_df[~test_df.reference_code.isin(MANUALLY_EXCLUDED_DUPLICATES)]\n",
+ " assert sum(test_df[((test_df[\"entry nr\"]==\"duplicate\") | (test_df[\"entry nr\"]==\"error\"))].id.isna())==0, (\"Duplicate or error found for an empty-ID row\", test_df[(((test_df[\"entry nr\"]==\"duplicate\") | (test_df[\"entry nr\"]==\"error\"))) & test_df.id.isna()])\n",
+ " ## Ensures that rows containing duplicate or error in entry nr column also has an appropriate ID.\n",
+ "\n",
+ "#print(\"I am removing the following duplicates and errors:\")\n",
+ "df = df[~((df[\"entry nr\"]==\"duplicate\") | (df[\"entry nr\"]==\"error\"))]\n",
+ "## Removes such rows"
+ ],
+ "metadata": {
+ "id": "qkoNWXhx_LQX"
+ },
+ "execution_count": null,
+ "outputs": []
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "#QC\n",
+ "if True:\n",
+ " ##check completeness of position annotation\n",
+ " na_counter = df[[\"part\",\"page\",\"col l/r\",\"table from top\", \"entry nr\"]].isna().sum(axis=\"columns\") ##Counts NaN values in position annotation\n",
+ " #print(na_counter)\n",
+ " assert len(df[~na_counter.isin([0,5])])==0, print(df[~na_counter.isin([0,5])][[\"id\",\"reference\",\"part\",\"page\",\"col l/r\",\"table from top\", \"entry nr\"]].to_string())\n",
+ " #Prints problematic rows if any\n",
+ "\n",
+ " ##Checks for spaces in /reference_code/ column.\n",
+ " assert len(df[df.reference_code.str.contains(\" \").fillna(False)])==0, print(df[df.reference_code.str.contains(\" \").fillna(False)].to_string())\n",
+ " ## And output problematic rows.\n",
+ "\n",
+ "## drop NaNs -- these entries just haven't been worked on and can't be checked\n",
+ "df = df.dropna(subset=[\"part\",\"page\",\"col l/r\",\"table from top\", \"entry nr\"])\n",
+ "\n",
+ "## convert values in columns part, page, col l/r, table from top and entry nr to integers\n",
+ "df[[\"part\",\"page\",\"col l/r\",\"table from top\", \"entry nr\"]] = df[[\"part\",\"page\",\"col l/r\",\"table from top\", \"entry nr\"]].astype(int)"
+ ],
+ "metadata": {
+ "colab": {
+ "base_uri": "https://localhost:8080/"
+ },
+ "id": "PwqHEVvMC3OC",
+ "outputId": "03d7517d-d10a-4226-a166-164f1e50ab5d"
+ },
+ "execution_count": null,
+ "outputs": [
+ {
+ "output_type": "stream",
+ "name": "stderr",
+ "text": [
+ ":10: FutureWarning: Downcasting object dtype arrays on .fillna, .ffill, .bfill is deprecated and will change in a future version. Call result.infer_objects(copy=False) instead. To opt-in to the future behavior, set `pd.set_option('future.no_silent_downcasting', True)`\n",
+ " assert len(df[df.reference_code.str.contains(\" \").fillna(False)])==0, print(df[df.reference_code.str.contains(\" \").fillna(False)].to_string())\n"
+ ]
+ }
+ ]
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "## quality check new data\n",
+ "\n",
+ "if True:\n",
+ " ## id is unique\n",
+ " assert len(df.dropna(subset=[\"id\"]).id.unique()) == len(df.dropna(subset=[\"id\"])), df.dropna(subset=[\"id\"])[df.dropna(subset=[\"id\"]).id.duplicated()].to_string()\n",
+ " ## Ensures that every value in column ID is unique, if not prints out problematic tows.\n",
+ "\n",
+ " ## tables intact in themselves\n",
+ "\n",
+ " ##Groups rows in dataframe by part, page, col l/r, and table from top values.\n",
+ "\n",
+ " for which, g in df.groupby([\"part\",\"page\",\"col l/r\",\"table from top\"]): # g is subset corresponding to specific part of the dataframe, as grouped by previously\n",
+ " #print((which,g))\n",
+ " #if which == (3, 1091, 1, 1):\n",
+ " # continue\n",
+ "\n",
+ " assert len(g.reference_code.unique())==1, (which, print(g.to_string())) ## Checks that all values in reference_code have the same value--\n",
+ " assert len(g.EC.unique()) == 1, (which, print(g.to_string())) ## Check that all EC values are uniform\n",
+ " assert len(g.reaction.unique())==1, (which, print(g.to_string())) ## - fixed \"description\" for correct column name\n",
+ " assert sorted(g[\"entry nr\"].values)==list(range(1,g[\"entry nr\"].max()+1)), (which, print(g.to_string())) ## Check that all values in entry nr are ordered from lowest to highest\n",
+ "\n",
+ " ## table counts consistently continuous\n",
+ " for which, g in df.groupby([\"part\", \"page\", \"col l/r\"]):\n",
+ " ## the following part/page/column combinations\n",
+ " #\n",
+ " # contain a table which was mentioned before;\n",
+ " ## the table is thus marked full duplicate and was removed beforehand; so we manually\n",
+ " ## exclude those from this automated check\n",
+ " MANUALLY_EXCLUDED_COLUMNS = [\n",
+ " (2, 558, 2),\n",
+ " (2, 560, 2),\n",
+ " (2, 566, 2),\n",
+ " (2, 584, 1),\n",
+ " (2, 590, 2),\n",
+ " (3, 1041, 1),\n",
+ " (3, 1076, 2),\n",
+ " (7, 1360, 2),\n",
+ " (7, 1369, 2),\n",
+ " (7, 1373, 1),\n",
+ " ]\n",
+ " ## shouldn't be necessary after introduction of duplicate_table column; so we use:\n",
+ " MANUALLY_EXCLUDED_COLUMNS = []\n",
+ " ## because there is a peculiarity about tables not-existent-in-the-pdf, but found in randr, we have to use:\n",
+ " MANUALLY_EXCLUDED_COLUMNS = [\n",
+ " (6, 948, 2),\n",
+ " (6, 949, 1),\n",
+ " ]\n",
+ " if which in MANUALLY_EXCLUDED_COLUMNS:\n",
+ " continue\n",
+ " assert sorted(g[\"table from top\"].unique()) == list(range(1, g[\"table from top\"].max() + 1)), (which, print(g.to_string())) # ensures that values in table from top are from lowest to highest\n",
+ "\n",
+ " ## column values either 1 or 2\n",
+ " for which, g in df.groupby([\"part\", \"page\"]):\n",
+ " assert all([i in [1,2] for i in g[\"col l/r\"].values]), (which, print(g.to_string())) # ensures that all values in col l/r are either 1 or 2\n",
+ "\n",
+ " ## page numbers consistently continuous\n",
+ " for which, g in df.groupby(\"part\"):\n",
+ " MANUALLY_EXCLUDED_PARTS = [\n",
+ " #2,\n",
+ " #3,\n",
+ " #7\n",
+ " ]\n",
+ " if which in MANUALLY_EXCLUDED_PARTS: #ensures that page numbers are continious by parts\n",
+ " continue\n",
+ "\n",
+ " print(f\"----- This is about part {which} -----\")\n",
+ " should_be = list(range(g[\"page\"].min(), g[\"page\"].max() + 1))\n",
+ " for page in should_be:\n",
+ " if page not in g[\"page\"].unique():\n",
+ " print(f\"Missing page: {page}\") #Finds missing pages and prints them out\n",
+ " #assert sorted(g[\"page\"].unique()) == list(range(g[\"page\"].min(), g[\"page\"].max() + 1))\n",
+ "\n",
+ "## extract added values\n",
+ "# print(f\"You will need to care for these {df.id.isna().sum()} recently added rows:\")\n",
+ "# print(df[df.id.isna()])\n",
+ "\n",
+ "print(\"The online spreadsheet data looks consistent.\")"
+ ],
+ "metadata": {
+ "colab": {
+ "base_uri": "https://localhost:8080/"
+ },
+ "id": "xUlWBY4aI8ri",
+ "outputId": "615d1079-f8ef-4e0a-cc78-30f0f2a4ff50"
+ },
+ "execution_count": null,
+ "outputs": [
+ {
+ "output_type": "stream",
+ "name": "stdout",
+ "text": [
+ "----- This is about part 1 -----\n",
+ "----- This is about part 2 -----\n",
+ "----- This is about part 3 -----\n",
+ "Missing page: 1088\n",
+ "Missing page: 1089\n",
+ "Missing page: 1090\n",
+ "----- This is about part 4 -----\n",
+ "----- This is about part 5 -----\n",
+ "----- This is about part 6 -----\n",
+ "----- This is about part 7 -----\n",
+ "The online spreadsheet data looks consistent.\n"
+ ]
+ }
+ ]
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "## consistency check between online spreadsheet and original Noor data\n",
+ "##Reading TECRDB and openTECR files\n",
+ "noor = pandas.read_csv(\"TECRDB.csv\")\n",
+ "noor = noor.rename(columns={\"reaction\": \"keggID\"})\n",
+ "noor = noor.rename(columns={\"reference\": \"reference_code\",'description':'reaction'})\n",
+ "## Updating column names in Noor set to match the new columns in openTECR.\n",
+ "if READ_CSV:\n",
+ " online = pandas.read_csv(\"openTECR recuration - actual data.csv\")\n",
+ "else:\n",
+ " online = pandas.read_excel(\"openTECR recuration.ods\", sheet_name=\"actual data\")\n",
+ "\n",
+ "\n",
+ "online = online.replace({\"col l/r\": {\"l\":1,\"r\":2}}) #replacing l/r values with 1 and 2\n",
+ "## check that all ids are still there\n",
+ "assert set(noor.id) - set(online.id) == set(), f\"The following IDs were deleted online: {set(noor.id)-set(online.id)}\"\n",
+ "## Checks that all ID are present in both openTECR and Noor\n",
+ "\n",
+ "## non-curated values should not have been changed by anyone!\n",
+ "leftjoined = pandas.merge(noor, online.dropna(subset=\"id\"), on=\"id\", how=\"left\", validate=\"1:1\")\n",
+ "## Merging noor set and openTECR together"
+ ],
+ "metadata": {
+ "id": "qogRI2yEodFu"
+ },
+ "execution_count": null,
+ "outputs": []
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "## This code snippet tries to check if K_prime values are equal in Noor and openTECR dataset\n",
+ "## While accounting for rounding up in openTECR\n",
+ "## If values are not equal despite being rounded up, it will output both k_prime values from noor and openTECR\n",
+ "## kPn is a prime_K column from Noor set roughly rounded up by the rules outlined in openTECR\n",
+ "\n",
+ "\n",
+ "\n",
+ "import numpy as np\n",
+ "kPn = []\n",
+ "for i in range(len(leftjoined.K_prime_x)):\n",
+ " if leftjoined.K_prime_x[i] != leftjoined.K_prime_y[i]:\n",
+ " if np.isnan(leftjoined.K_prime_x[i]) == False:\n",
+ " #print(leftjoined.K_prime_x[i])\n",
+ " #print(leftjoined.K_prime_y[i])\n",
+ " ##Trying to match weird rounding up format of openTECR Kprime values\n",
+ " if len(str(leftjoined.K_prime_x[i]).split('.')[1])>4:\n",
+ " rounded = round(leftjoined.K_prime_x[i],len(str(leftjoined.K_prime_x[i]).split('.')[1])-1)\n",
+ " #print(rounded)\n",
+ " elif len(str(leftjoined.K_prime_x[i]).split('.')[1])==2:\n",
+ " rounded = round(leftjoined.K_prime_x[i],1)\n",
+ " #print(rounded)\n",
+ " elif len(str(leftjoined.K_prime_x[i]).split('.')[1])==3:\n",
+ " rounded = round(leftjoined.K_prime_x[i], 2)\n",
+ " #print(rounded)\n",
+ " elif len(str(leftjoined.K_prime_x[i]).split('.')[1])==1:\n",
+ " rounded = round(leftjoined.K_prime_x[i], 0)\n",
+ " #print(rounded)\n",
+ " #print(round(leftjoined.K_prime_x[i], 2))\n",
+ " if rounded+0.1 == leftjoined.K_prime_y[i]:\n",
+ " kPn.append(rounded+0.1)\n",
+ " else:\n",
+ " kPn.append(rounded)\n",
+ " else:\n",
+ " kPn.append(leftjoined.K_prime_x[i])\n",
+ " else:\n",
+ " kPn.append(leftjoined.K_prime_x[i])\n",
+ "for i in range(len(leftjoined.K_prime_y)):\n",
+ " if kPn[i] != leftjoined.K_prime_y[i]:\n",
+ " if np.isnan(leftjoined.K_prime_y[i]) == False:\n",
+ " print(f'Noor set K_prime value: {kPn[i]}')\n",
+ " print(f'openTECR set K_prime value: {leftjoined.K_prime_y[i]}')\n",
+ "## Some cases couldn't be handled since they don't follow rounding logic"
+ ],
+ "metadata": {
+ "id": "SXZzIqZZohFH"
+ },
+ "execution_count": null,
+ "outputs": []
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "## Columns that should be the same\n",
+ "SHOULD_BE_THE_SAME = [\n",
+ " \"reference_code\",\n",
+ " \"EC\",\n",
+ " \"reaction\",\n",
+ " \"K\",\n",
+ " \"temperature\",\n",
+ " \"ionic_strength\",\n",
+ " \"p_h\",\n",
+ " \"p_mg\",\n",
+ " #\"K_prime\", # - checked manually, weird rounding up in online data? Handled by code above\n",
+ "]\n",
+ "for s in SHOULD_BE_THE_SAME:\n",
+ " entries_where_both_are_nans = leftjoined[ leftjoined[f\"{s}_x\"].isna() & leftjoined[f\"{s}_y\"].isna() ]\n",
+ " if len(entries_where_both_are_nans) == 0:\n",
+ " assert (leftjoined[f\"{s}_x\"] == leftjoined[f\"{s}_y\"]).all(), (s, print(leftjoined[~(leftjoined[f\"{s}_x\"] == leftjoined[f\"{s}_y\"])][[\"id\",f\"{s}_x\",f\"{s}_y\"]].to_string()))\n",
+ " else:\n",
+ " tmp = leftjoined[ ~ (leftjoined[f\"{s}_x\"].isna() & leftjoined[f\"{s}_y\"].isna()) ]\n",
+ " assert (tmp[f\"{s}_x\"] == tmp[f\"{s}_y\"]).all(), (s, print(tmp[~(tmp[f\"{s}_x\"] == tmp[f\"{s}_y\"])][[\"id\",f\"{s}_x\",f\"{s}_y\"]].to_string()))\n",
+ "\n",
+ "## The code above checks that all values in those columns between both Noor (_x) and openTECR (_y) are either NaN or equal. If not, raises assertion error and prints out incorrect rows\n",
+ "\n",
+ "## did someone add a new row without id, where they should have corrected a row with id?\n",
+ "merged = pandas.merge(online, noor, on=[\n",
+ " \"reference_code\",\n",
+ " \"temperature\",\n",
+ " \"ionic_strength\",\n",
+ " \"p_h\",\n",
+ " \"p_mg\",\n",
+ " \"K_prime\",\n",
+ "])\n",
+ "merged = merged[merged[\"id_x\"] != merged[\"id_y\"]]\n",
+ "potential_errors = merged[merged[\"id_x\"].isna() | merged[\"id_y\"].isna()]\n",
+ "\n",
+ "## Checks whether or not noor and online set have matching ID values\n",
+ "\n",
+ "## the following have been manually checked to be able to be excluded from the comparison below:\n",
+ "MANUALLY_EXCLUDED = [\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4356\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1714\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1715\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1716\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1718\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1717\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2140\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2149\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3167\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3184\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry707\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4246\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry392\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1269\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4283\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4284\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3888\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3896\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3897\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1915\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1603\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1605\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry236\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry386\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2718\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3560\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3561\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4006\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1271\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1586\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1589\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1590\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1591\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1588\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1587\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2370\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2371\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1601\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3637\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2725\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry705\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry702\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry704\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4040\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4373\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1829\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3031\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3032\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2339\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry1916\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3026\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4086\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2848\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry4316\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry772\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2851\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry398\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry82\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry806\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry805\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry3654\",\n",
+ " \"https://w3id.org/related-to/doi.org/10.5281/zenodo.3978439/files/TECRDB.csv#entry2277\",\n",
+ "]\n",
+ "potential_errors = potential_errors[ ~potential_errors.id_y.isin(MANUALLY_EXCLUDED) ]\n",
+ "if len(potential_errors) > 0:\n",
+ " print(\"The following entries might have been added as a new row without id, where they should have corrected a row with id:\")\n",
+ " print(potential_errors.to_string())\n",
+ "\n",
+ "print(\"The online spreadsheet data and its original data source are still in sync.\")"
+ ],
+ "metadata": {
+ "colab": {
+ "base_uri": "https://localhost:8080/"
+ },
+ "id": "6-RFQB1zgc2N",
+ "outputId": "17acfa5d-6058-4928-e7d1-5e4069772ca1"
+ },
+ "execution_count": null,
+ "outputs": [
+ {
+ "output_type": "stream",
+ "name": "stdout",
+ "text": [
+ "The online spreadsheet data and its original data source are still in sync.\n"
+ ]
+ }
+ ]
+ },
+ {
+ "cell_type": "code",
+ "source": [
+ "\n",
+ "## annotate online spreadsheet with table_codes\n",
+ "#\n",
+ "#\n",
+ "## read second df\n",
+ "## -- get it manually from https://zenodo.org/record/5495826 !\n",
+ "noor = pandas.read_csv(\"TECRDB.csv\")\n",
+ "noor.columns\n",
+ "#Index(['id', 'url', 'reference', 'method', 'eval', 'EC', 'enzyme_name',\n",
+ "# 'reaction', 'description', 'K', 'K_prime', 'temperature',\n",
+ "# 'ionic_strength', 'p_h', 'p_mg'],\n",
+ "\n",
+ "noor = noor.drop(['K', 'K_prime', 'temperature',\n",
+ " 'ionic_strength', 'p_h', 'p_mg'],axis=\"columns\")\n",
+ "\n",
+ "## Fixed to matching name in openTECR\n",
+ "noor = noor.rename(columns={\"reaction\": \"keggID\"})\n",
+ "noor = noor.rename(columns={\"reference\": \"reference_code\",'description':'reaction'})\n",
+ "\n",
+ "## extract table codes\n",
+ "noor[\"table_code\"] = noor.url.str.split(\"&T1=\").str[-1]\n",
+ "\n",
+ "## quality check\n",
+ "if True:\n",
+ " ## tables intact in themselves\n",
+ " for which, g in noor.groupby(\"table_code\"):\n",
+ " #print((which,g))\n",
+ " assert len(g.reference_code.unique())==1, (which, print(g.to_string()))\n",
+ " assert len(g.method.unique())==1, (which, print(g.to_string()))\n",
+ " assert len(g[\"eval\"].unique()) == 1, (which, print(g.to_string()))\n",
+ " assert len(g.EC.unique()) == 1, (which, print(g.to_string()))\n",
+ " assert len(g.enzyme_name.unique())==1, (which, print(g.to_string()))\n",
+ " assert len(g.reaction.unique()) == 1, (which, print(g.to_string()))\n",
+ " assert len(g.reaction.unique()) == 1, (which, print(g.to_string()))\n",
+ "\n",
+ "## Ensures that all values in those columns are consistent\n",
+ "\n",
+ "## drop now-unnecessary columns\n",
+ "noor = noor.drop([\"EC\",\"reference_code\", \"reaction\"], axis=\"columns\")\n",
+ "#df = df.drop( [\"description\"], axis=\"columns\")\n",
+ "\n",
+ "## merge\n",
+ "tmp = pandas.merge(df, noor, how=\"left\", on=\"id\")\n",
+ "\n",
+ "## add manually extracted table codes\n",
+ "if READ_CSV:\n",
+ " manual_table_codes = pandas.read_csv(\"openTECR recuration - table codes.csv\")\n",
+ "else:\n",
+ " manual_table_codes = pandas.read_excel(\"openTECR recuration.ods\", sheet_name=\"manually mapped table codes\")\n",
+ "\n",
+ "# QC\n",
+ "if True:\n",
+ " assert sum(manual_table_codes.duplicated([\"part\", \"page\", \"col l/r\", \"table from top\"])) == 0, print(\n",
+ " manual_table_codes[manual_table_codes.duplicated([\"part\", \"page\", \"col l/r\", \"table from top\"])])\n",
+ "# split into tables with table codes from Noor and those which needed to be annotated manually\n",
+ "manual_table_codes = manual_table_codes.drop([\"reference\", \"description\"], axis=\"columns\")\n",
+ "tmp_with_table_codes = tmp[~tmp.table_code.isna()]\n",
+ "tmp_without_table_codes = tmp[tmp.table_code.isna()]\n",
+ "tmp_without_table_codes = tmp_without_table_codes.drop(\"table_code\", axis=\"columns\")\n",
+ "tmp_without_table_codes_try_to_add_manual_ones = pandas.merge(tmp_without_table_codes, manual_table_codes, how=\"left\", on=[\"part\",\"page\",\"col l/r\",\"table from top\"])\n",
+ "# concat the two\n",
+ "new = pandas.concat([tmp_with_table_codes, tmp_without_table_codes_try_to_add_manual_ones], ignore_index=True)\n",
+ "## keep only one entry per table code, remove now-meaningless columns, but keep id=NaN rows\n",
+ "new = new[~new.duplicated([\"part\",\"page\",\"col l/r\",\"table from top\"])]\n",
+ "new = new.drop([\"id\",\"url\"], axis=\"columns\")\n",
+ "new[\"comment\"] = \"\"\n",
+ "\n",
+ "## Ensures no diplicate values in manual_table_codes\n",
+ "## Splits tmp into portitions with and without table_codes\n",
+ "## Removes duplicate entries and adds column \"comment\" for further annotation\n",
+ "\n",
+ "## export tables which need to be added to the \"table codes\" tab\n",
+ "selector = []\n",
+ "for i,s in new.iterrows():\n",
+ " if pandas.isna(s.table_code):\n",
+ " if len(manual_table_codes[(manual_table_codes.part == s.part) &\n",
+ " (manual_table_codes.page == s.page) &\n",
+ " (manual_table_codes[\"col l/r\"] == s[\"col l/r\"]) &\n",
+ " (manual_table_codes[\"table from top\"] == s[\"table from top\"])\n",
+ " ]) == 0:\n",
+ " selector.append(i)\n",
+ "export = new.loc[selector]\n",
+ "(export[[\n",
+ " \"part\",\"page\",\"col l/r\",\"table from top\",\n",
+ " \"table_code\",\n",
+ " \"reaction\",\n",
+ " \"reference_code\",\n",
+ " \"curator\",\n",
+ " ]]\n",
+ " .sort_values([\"part\",\"page\",\"col l/r\",\"table from top\"])\n",
+ " .to_csv(\"2024-01-06-opentecr-recuration.missing_table_codes.csv\", index=False)\n",
+ " )\n",
+ "\n",
+ "## identifies and exports rows from the new DataFrame that are missing table_code values and do not already exist in manual_table_codes, creating a CSV file with them\n",
+ "## selector - rows that need to be exported\n",
+ "\n",
+ "\n",
+ "## export tables which need to have their comment extracted\n",
+ "selector = []\n",
+ "if READ_CSV:\n",
+ " tables_with_comments = pandas.read_csv(\"openTECR recuration - table metadata.csv\")\n",
+ "else:\n",
+ " tables_with_comments = pandas.read_excel(\"openTECR recuration.ods\", sheet_name=\"table comments\")\n",
+ "## QC\n",
+ "if True:\n",
+ " assert sum(tables_with_comments.duplicated([\"part\",\"page\",\"col l/r\",\"table from top\"]))==0, print(tables_with_comments[tables_with_comments.duplicated([\"part\",\"page\",\"col l/r\",\"table from top\"])])\n",
+ "\n",
+ "# Identify rows in new df that are not present in the metadata\n",
+ "for i, s in new.iterrows():\n",
+ " # Check if a matching entry exists in `tables_with_comments`\n",
+ " if len(tables_with_comments[\n",
+ " (tables_with_comments.part == s.part) &\n",
+ " (tables_with_comments.page == s.page) &\n",
+ " (tables_with_comments[\"col l/r\"] == s[\"col l/r\"]) &\n",
+ " (tables_with_comments[\"table from top\"] == s[\"table from top\"])\n",
+ " ]) == 0:\n",
+ " # If no match is found, add the index of the row to `selector`\n",
+ " selector.append(i)\n",
+ "\n",
+ "tables_without_comments = new.loc[selector]\n",
+ "# Add placeholders for manual annotation and spellchecking\n",
+ "tables_without_comments[\"manually spellchecked\"] = \"\"\n",
+ "tables_without_comments[\"comment\"] = \"\"\n",
+ "\n",
+ "\n",
+ "# Export the filtered data to a CSV file\n",
+ "\n",
+ "(tables_without_comments[[\n",
+ " \"part\",\"page\",\"col l/r\",\"table from top\",\n",
+ " \"reference_code\",\n",
+ " \"manually spellchecked\",\n",
+ " \"comment\"\n",
+ " ]]\n",
+ " .sort_values([\"part\",\"page\",\"col l/r\",\"table from top\"])\n",
+ " .to_csv(\"2024-01-06-opentecr-recuration.missing-table-comments.csv\", index=False)\n",
+ " )\n",
+ "\n",
+ "print(\"I could merge the online spreadsheet and the Noor data. I have written file regarding the tables to your disk.\")"
+ ],
+ "metadata": {
+ "id": "9pjJJF2TX0rl"
+ },
+ "execution_count": null,
+ "outputs": []
+ }
+ ]
+}
\ No newline at end of file