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Volumn 277, Issue 14, 2002, Pages 12175-12181
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The COOH terminus of arylamine N-acetyltransferase from Salmonella typhimurium controls enzymic activity
a
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Author keywords
[No Author keywords available]
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Indexed keywords
AMINO ACIDS;
DIMERS;
DRUG PRODUCTS;
ENZYMES;
ESCHERICHIA COLI;
HYDROLYSIS;
MONOMERS;
CRYSTAL UNIT CELLS;
BIOCHEMISTRY;
ACETIC ACID DERIVATIVE;
ACETYL COENZYME A;
AROMATIC AMINE;
ARYLAMINE ACETYLTRANSFERASE;
ASPARTIC ACID;
CYSTEINE;
CYSTEINE PROTEINASE;
DIMER;
HISTIDINE;
HYDRAZINE DERIVATIVE;
HYDROLASE;
HYDROXYLAMINE;
ISONIAZID;
MONOMER;
MUTANT PROTEIN;
TETRAMER;
TUBERCULOSTATIC AGENT;
ACETYLATION;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
CONTROLLED STUDY;
CRYSTAL STRUCTURE;
CYTOTOXICITY;
DRUG INACTIVATION;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME STRUCTURE;
ESCHERICHIA COLI;
HYDROLYSIS;
NONHUMAN;
PRIORITY JOURNAL;
SALMONELLA TYPHIMURIUM;
SEQUENCE HOMOLOGY;
AMINES;
AMINO ACID SEQUENCE;
ARYLAMINE N-ACETYLTRANSFERASE;
BINDING SITES;
CATALYSIS;
CLONING, MOLECULAR;
CYTOSOL;
ESCHERICHIA COLI;
HYDROLYSIS;
KINETICS;
MODELS, CHEMICAL;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTATION;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, TERTIARY;
RECOMBINANT PROTEINS;
SALMONELLA TYPHIMURIUM;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
SALMONELLA TYPHIMURIUM;
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EID: 0037023704
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M104365200 Document Type: Article |
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Times cited : (69)
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References (50)
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