Arylamine N-acetyltransferase I

Rodney F. Minchin, Patrick E. Hanna, Jean Marie Dupret, Carston R. Wagner, Fernando Rodrigues-Lima, Neville J. Butcher

Research output: Contribution to journalShort surveypeer-review

60 Scopus citations

Abstract

Arylamine N-acetyltransferase I (NAT1) is a phase II enzyme that acetylates a wide range of arylamine and hydrazine substrates. The NAT1 gene is located on chromosome 8 and shares homology to NAT genes found in most mammalian species. Gene expression occurs from at least two promoters and a number of tissue-specific transcripts have been identified. The gene is polymorphic with most mutations identified to date producing an unstable protein that is subject to polyubiquitination. The NAT1 protein contains a catalytic triad similar to a number of cysteine proteases and transglutaminases. NAT1 is widely distributed in the body, but the only endogenous substrate identified to date is the folate catabolite p-aminobenzoylglutamate. Recent links between NAT1 genotypes and susceptibility to spina bifida suggests that the enzyme has an important role in folate homeostasis.

Original languageEnglish (US)
Pages (from-to)1999-2005
Number of pages7
JournalInternational Journal of Biochemistry and Cell Biology
Volume39
Issue number11
DOIs
StatePublished - Sep 11 2007

Keywords

  • Arylamine N-acetyltransferase
  • Catalytic triad
  • Folate metabolism
  • Polymorphism
  • Ubiquitination

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