Journal
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume 1620, Issue 1-3, Pages 8-14Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0304-4165(02)00500-7
Keywords
nuclear magnetic resonance; arylamine N-acetyltransferase; isoniazid; drug metabolism; carcinogenesis
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Arylamine N-acetyltransferases (NAT) are a family of enzymes found in both eucaryotes and procaryotes, which catalyse the N-acetylation of a range of arylamine and hydrazine drugs and carcinogenic arylamines, using acetyl Coenzyme A as a cofactor. Here we describe a nuclear magnetic resonance (NMR) investigation of the interaction of substrates with Salmonella typhimurium NAT. For solution NMR investigations, pure recombinant NAT from S. typhimurium was used at up to 0.1 mM. We demonstrate that a hydrazine substrate, isoniazid (m), binds to the protein in the absence of the cofactor, acetyl CoA, and thereby suggest that even though the catalysis may follow a ping-pong pathway, ligand-enzyme interactions can occur in the absence of acetyl CoA. (C) 2002 Elsevier Science B.V All rights reserved.
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