Kinetic characterisation of arylamine N-acetyltransferase from Pseudomonas aeruginosa |
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Authors: | Isaac M Westwood Edith Sim |
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Affiliation: | (1) Department of Pharmacology, University of Oxford, Mansfield Road, Oxford, UK |
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Abstract: | Background Arylamine N-acetyltransferases (NATs) are important drug- and carcinogen-metabolising enzymes that catalyse the transfer of an acetyl group from a donor, such as acetyl coenzyme A, to an aromatic or heterocyclic amine, hydrazine, hydrazide or N-hydroxylamine acceptor substrate. NATs are found in eukaryotes and prokaryotes, and they may also have an endogenous function in addition to drug metabolism. For example, NAT from Mycobacterium tuberculosis has been proposed to have a role in cell wall lipid biosynthesis, and is therefore of interest as a potential drug target. To date there have been no studies investigating the kinetic mechanism of a bacterial NAT enzyme. |
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