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Volumn 128, Issue 4, 2000, Pages 679-686
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Stereochemistry of the transamination reaction catalyzed by aminodeoxychorismate lyase from Escherichia coli: Close relationship between fold type and stereochemistry
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Author keywords
Aminodeoxychorismate lyase; Molecular evolution; Pyridoxal 5' phosphate; Stereochemistry; Transamination
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Indexed keywords
AMINODEOXYCHORISMATE LYASE;
AMINOTRANSFERASE;
CHORISMIC ACID;
LYASE;
PYRIDOXAL 5 PHOSPHATE;
UNCLASSIFIED DRUG;
ARTICLE;
CATALYSIS;
ENZYME SPECIFICITY;
ENZYME SUBSTRATE;
ESCHERICHIA COLI;
MOLECULAR EVOLUTION;
PROTEIN FAMILY;
PROTEIN SECONDARY STRUCTURE;
PROTON TRANSPORT;
REACTION ANALYSIS;
STEREOCHEMISTRY;
TRANSAMINATION;
X RAY CRYSTALLOGRAPHY;
ALANINE;
APOENZYMES;
CATALYSIS;
ESCHERICHIA COLI;
EVOLUTION, MOLECULAR;
HYDROGEN;
KINETICS;
MOLECULAR CONFORMATION;
OXO-ACID-LYASES;
PROTEIN FOLDING;
PYRIDOXAL PHOSPHATE;
PYRIDOXAMINE;
PYRUVIC ACID;
RECOMBINANT PROTEINS;
SPECTROPHOTOMETRY;
TRANSAMINASES;
TRYPTOPHAN SYNTHASE;
TRYPTOPHANASE;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
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EID: 0033780490
PISSN: 0021924X
EISSN: None
Source Type: Journal
DOI: 10.1093/oxfordjournals.jbchem.a022801 Document Type: Article |
Times cited : (14)
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References (36)
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