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Publication Type
Journal Article
UWI Author(s)
Author, Analytic
Delgoda, Rupika; Lian, Lu-Yun; Sandy, James; Sim, Edith
Author Affiliation, Ana.
Natural Products Institute
Article Title
NMR investigation of the catalytic mechanism of arylamine N-acetyltransferases from Salmonella typhimurium
Medium Designator
n/a
Connective Phrase
n/a
Journal Title
Biochemica et biophysica acta
Translated Title
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Reprint Status
n/a
Date of Publication
2003
Volume ID
1620
Issue ID
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Page(s)
8-14
Language
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Connective Phrase
n/a
Location/URL
www.sciencedirect.com
ISSN
n/a
Notes
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Abstract
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 (INH), 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.....
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