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Volume 147, Issue 5

Eubacterial arylamine -acetyltransferases – identification and comparison of 18 members of the protein family with conserved active site cysteine, histidine and aspartate residues Free

Abstract

Arylamine -acetyltransferases (NATs) are enzymes involved in the detoxification of a range of arylamine and hydrazine-based xenobiotics. NATs have been implicated in the endogenous metabolism of -aminobenzoyl glutamate in eukaryotes, although very little is known about the distribution and function of NAT in the prokaryotic kingdom. Using DNA library screening techniques and the analysis of data from whole-genome sequencing projects, we have identified 18 -like sequences from the and . Recently, the three-dimensional structure of NAT derived from the bacterium (PDB accession code 1E2T) was resolved and revealed an active site catalytic triad composed of Cys-His-Asp. These residues have been shown to be conserved in all prokaryotic and eukaryotic NAT homologues together with three highly conserved regions which are found proximal to the active site triad. The characterization of prokaryotic NATs and NAT-like enzymes is reported. It is also predicted that prokaryotic NATs, based on gene cluster composition and distribution amongst genomes, participate in the metabolism of xenobiotics derived from decomposition of organic materials.

  • Received:
  • Accepted:
  • Revised:
  • Published Online:
Keyword(s): endogenous function , gene cluster , INH, isoniazid , NAT , NAT, arylamine N-acetyltransferase encoded by nat in prokaryotes and NAT in eukaryotes , p-ABA, p-aminobenzoic acid , prokaryotic and RAS, rifamycin amide synthase
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2001-05-01
2024-04-26
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Eubacterial arylamine N-acetyltransferases – identification and comparison of 18 members of the protein family with conserved active site cysteine, histidine and aspartate residues
Microbiology 147, 1137 (2001); https://doi.org/10.1099/00221287-147-5-1137
/content/journal/micro/10.1099/00221287-147-5-1137
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