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Volumn 41, Issue 5, 2002, Pages 1421-1427
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Kinetic and mechanistic analysis of the malonyl CoA:ACP transacylase from Streptomyces coelicolor indicates a single catalytically competent serine nucleophile at the active site
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Author keywords
[No Author keywords available]
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Indexed keywords
MALONYLATION;
BIOSYNTHESIS;
CATALYSIS;
ENZYME KINETICS;
FATTY ACIDS;
ESCHERICHIA COLI;
ACYL CARRIER PROTEIN;
ACYL CARRIER PROTEIN TRANSACYLASE;
ACYLTRANSFERASE;
FATTY ACID;
FATTY ACID SYNTHASE;
HEXAHISTIDINE;
HISTIDINE;
HYBRID PROTEIN;
MALONYL COENZYME A;
POLYKETIDE;
SYNTHETASE;
UNCLASSIFIED DRUG;
ARTICLE;
BIOSYNTHESIS;
CATALYSIS;
CONTROLLED STUDY;
ENZYME ACTIVE SITE;
ESCHERICHIA COLI;
INCUBATION TIME;
KINETICS;
MEASUREMENT;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN EXPRESSION;
STREPTOMYCES COELICOLOR;
3-OXOACYL-(ACYL-CARRIER-PROTEIN) SYNTHASE;
ACYL CARRIER PROTEIN;
ACYL-CARRIER PROTEIN S-MALONYLTRANSFERASE;
ACYLTRANSFERASES;
BINDING SITES;
CATALYSIS;
CLONING, MOLECULAR;
FATTY ACID SYNTHETASE COMPLEX;
KINETICS;
MUTAGENESIS, SITE-DIRECTED;
SERINE;
STREPTOMYCES;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
STREPTOMYCES;
STREPTOMYCES COELICOLOR;
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EID: 0037022193
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi012001p Document Type: Article |
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Times cited : (41)
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References (21)
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