Structural investigation of mutant Mycobacterium smegmatis arylamine N-acetyltransferase: a model for a naturally occurring functional polymorphism in Mycobacterium tuberculosis arylamine N-acetyltransferase.

Journal article

Arylamine N-acetyltransferase (NAT) acetylates the front-line anti-tuberculosis drug isoniazid (INH) and has been identified in Mycobacterium tuberculosis. A naturally occurring single nucleotide polymorphism (SNP) was recently found in the NAT gene in clinical isolates of M. tuberculosis. The nucleotide change from G-->A (619) produces an amino acid change Gly(207) Arg, which appears to reduce the activity of the NAT from M. tuberculosis (TBNAT). It has not been possible to generate suffi...

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Authors: Kawamura, A; Sandy, J; Upton, A; Noble, M; Sim, E

• Publication status: Published
• Journal: Protein expression and purification
• Volume: 27
• Issue: 1
• Pages: 75-84
• Publication date: 2003-01-01
• DOI: 10.1016/s1046-5928(02)00592-2
• EISSN: 1096-0279
• ISSN: 1046-5928
• Language: English
• Keywords: Arylamine N-Acetyltransferase; Models, Molecular; Protein Conformation; Mycobacterium tuberculosis; Protein Denaturation; Amino Acid Sequence; Molecular Sequence Data; Crystallization; Kinetics; Mutation; Enzyme Stability; Temperature; Recombinant Proteins; Circular Dichroism; Polymorphism, Single Nucleotide; Mycobacterium smegmatis