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Volumn 267, Issue 19, 2000, Pages 5967-5976
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The role of Glu74 and Tyr82 in the reaction catalyzed by sheep liver cytosolic serine hydroxymethyltransferase
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Author keywords
Active site residues; Conformational change; Proton abstraction; Serine hydroxymethyltransferase; Spectral intermediates
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Indexed keywords
ACETAL DERIVATIVE;
ALANINE;
DIHYDROFOLATE REDUCTASE;
FORMALDEHYDE;
GLUTATHIONE;
GLYCINE HYDROXYMETHYLTRANSFERASE;
RECOMBINANT ENZYME;
SERINE;
THREONINE;
TYROSINE;
ARTICLE;
CHEMICAL BOND;
CONFORMATIONAL TRANSITION;
CRYSTAL STRUCTURE;
ENZYME ACTIVITY;
ENZYME MECHANISM;
ENZYME SPECIFICITY;
ENZYME SUBSTRATE;
LIVER CYTOSOL;
NONHUMAN;
PRIORITY JOURNAL;
SHEEP;
TRANSAMINATION;
ALANINE;
AMINO ACID SUBSTITUTION;
ANIMALS;
APOENZYMES;
BINDING SITES;
CALORIMETRY, DIFFERENTIAL SCANNING;
CATALYSIS;
CYTOSOL;
FORMALDEHYDE;
GLUTAMIC ACID;
GLYCINE HYDROXYMETHYLTRANSFERASE;
HUMANS;
KINETICS;
LIVER;
MUTAGENESIS, SITE-DIRECTED;
PYRIDOXAL PHOSPHATE;
RABBITS;
RECOMBINANT FUSION PROTEINS;
SERINE;
SHEEP;
STRUCTURE-ACTIVITY RELATIONSHIP;
TETRAHYDROFOLATES;
TYROSINE;
ORYCTOLAGUS CUNICULUS;
OVIS ARIES;
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EID: 0033807968
PISSN: 00142956
EISSN: None
Source Type: Journal
DOI: 10.1046/j.1432-1327.2000.01667.x Document Type: Article |
Times cited : (30)
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References (28)
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