The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis - An enzyme which inactivates the anti-tubercular drug, isoniazid

Journal of Molecular Biology

Volumn 318, Issue 4, 2002, Pages 1071-1083

  Sandy, James ^a   Mushtaq, Adeel ^a   Kawamura, Akane ^a   Sinclair, John ^a   Sim, Edith ^a   Noble, Martin ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Arylamine N acetyltransferase; Catalytic triad; Mycobacteria; TB; X ray crystallography

Indexed keywords

ALCOHOL DERIVATIVE; ARYLAMINE ACETYLTRANSFERASE; CYSTEINE PROTEINASE; ISONIAZID; THIOL DERIVATIVE; TUBERCULOSTATIC AGENT;

ARTICLE; CATALYSIS; DRUG DESIGN; DRUG INACTIVATION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STRUCTURE; GEOMETRY; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; SALMONELLA TYPHIMURIUM; STRUCTURE ANALYSIS;

BACTERIA (MICROORGANISMS); CORYNEBACTERINEAE; MYCOBACTERIUM; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; SALMONELLA TYPHIMURIUM;

EID: 0036042103     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00141-9     Document Type: Article

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