Kinetic and chemical mechanism of arylamine N-acetyltransferase from Mycobacterium tuberculosis

Biochemistry

Volumn 47, Issue 40, 2008, Pages 10781-10789

  Sikora, Alison L ^a   Frankel, Brenda A ^a   Blanchard, John S ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDS; AMINATION; AMINES; ENZYMES; HYDRAZINE; ORGANIC POLYMERS;

3-AMINO-4-HYDROXYBENZOIC ACID; ACETYL COENZYME A; ACETYL GROUPS; AMINO GROUPS; ARYL-AMINES; ARYLAMINE N-ACETYLTRANSFERASES; CHEMICAL MECHANISMS; CYTOSOLIC ENZYMES; ISONIAZID RESISTANCE; KINETIC CHARACTERIZATION; M. TUBERCULOSIS; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; N-ACETYLTRANSFERASE; OVER-EXPRESSION; PRODRUG; SUBSTITUTED ANILINES;

SUBSTRATES;

3 AMINO 4 HYDROXYBENZOIC ACID; ANILINE DERIVATIVE; ARYLAMINE ACETYLTRANSFERASE; BENZOIC ACID DERIVATIVE; HYDRAZINE DERIVATIVE; ISONIAZID; UNCLASSIFIED DRUG;

ACETYLATION; ANTIBIOTIC RESISTANCE; ARTICLE; CATALYSIS; CHEMICAL REACTION KINETICS; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SUBSTRATE; GENE OVEREXPRESSION; GENE TRANSFER; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PH MEASUREMENT; PRIORITY JOURNAL; PROTON TRANSPORT; SOLVENT EFFECT; STEADY STATE;

ARYLAMINE N-ACETYLTRANSFERASE; BACTERIAL PROTEINS; CATALYSIS; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, BIOLOGICAL; MOLECULAR STRUCTURE; MYCOBACTERIUM TUBERCULOSIS; SUBSTRATE SPECIFICITY;

MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS;

EID: 53249149273     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800398c     Document Type: Article

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