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Article

Divergence of cofactor recognition across evolution: coenzyme A binding in a prokaryotic arylamine N-acetyltransferase.

Journal of molecular biology - 4 Jan 2008

Fullam Elizabeth, Westwood Isaac M, Anderton Matthew C, Lowe Edward D, Sim Edith, Noble Martin E M

Abstract excerpt

Arylamine N-acetyltransferase (NAT) enzymes are widespread in nature. They serve to acetylate xenobiotics and/or endogenous substrates using acetyl coenzyme A (CoA) as a cofactor. Conservation of the architecture of the NAT enzyme family from mammals to bacteria has been demonstrated by a series of prokaryotic NAT structures, together with the recently reported structure of human NAT1. We report here the cloning,...

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Source

Identifiers

PMID: 18005984
DOI: 10.1016/j.jmb.2007.10.019

Genes

NAT1
NAT2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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