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Volumn 40, Issue 42, 2001, Pages 12497-12504
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Dehydration is catalyzed by glutamate-136 and aspartic acid-135 active site residues in Escherichia coli dTDP-glucose 4,6-dehydratase
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Author keywords
[No Author keywords available]
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Indexed keywords
PROTONATION;
CATALYSIS;
DEHYDRATION;
DEHYDROGENATION;
ENZYME KINETICS;
ESCHERICHIA COLI;
COENZYMES;
ASPARTIC ACID;
DEUTERIUM;
FLUORIDE ION;
GLUTAMIC ACID;
HYDROLYASE;
SOLVENT;
THYMIDINE DIPHOSPHATE;
THYMIDINE DIPHOSPHATE 4 KETO 6 DEOXYGLUCOSE;
THYMIDINE DIPHOSPHATE 6 FLUORO 6 DEOXYGLUCOSE;
THYMIDINE DIPHOSPHATE GLUCOSE 4,6 DEHYDRATASE;
UNCLASSIFIED DRUG;
XYLOSE;
ARTICLE;
CATALYSIS;
CHEMICAL REACTION;
DEHYDRATION;
DISSOCIATION CONSTANT;
ENZYME ACTIVE SITE;
ESCHERICHIA COLI;
NONHUMAN;
PRIORITY JOURNAL;
PROTON TRANSPORT;
REACTION ANALYSIS;
STEADY STATE;
ASPARTIC ACID;
BINDING SITES;
CATALYSIS;
DEOXYGLUCOSE;
ESCHERICHIA COLI;
GLUTAMIC ACID;
HYDRO-LYASES;
HYDROGEN;
HYDROGEN-ION CONCENTRATION;
KINETICS;
PROTONS;
SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;
SUBSTRATE SPECIFICITY;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
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EID: 0035940447
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi011138c Document Type: Article |
Times cited : (28)
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References (27)
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