ArticleThe Biochemical journal2001
Homology modelling and structural analysis of human arylamine N-acetyltransferase NAT1: evidence for the conservation of a cysteine protease catalytic domain and an active-site loop.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 58 citations in OpenAlex.
- HumanFrontiers in pharmacology · 2022Article
- Structural and biochemical characterization of an active arylamine N-acetyltransferase possessing a non-canonical Cys-His-Glu catalytic triad.The Journal of biological chemistry · 2013Article
- Structure of the cyclomodulin Cif from pathogenic Escherichia coli.Journal of molecular biology · 2008Article
- Arylamine N-acetyltransferases: a new inhibitor of apoptosis in HepG2 cells.Journal of Zhejiang University. Science. B · 2008Article
- Structure/function evaluations of single nucleotide polymorphisms in human N-acetyltransferase 2.Current drug metabolism · 2008Review
- Computational and experimental analyses of mammalian arylamine N-acetyltransferase structure and function.Drug metabolism and disposition: the biological fate of chemicals · 2007Article
- Kinetic characterisation of arylamine N-acetyltransferase from Pseudomonas aeruginosa.BMC biochemistry · 2007Article
- Functional characterization of the A411T (L137F) and G364A (D122N) genetic polymorphisms in human N-acetyltransferase 2.Pharmacogenetics and genomics · 2007Article
- Identification and characterization of functional rat arylamine N-acetyltransferase 3: comparisons with rat arylamine N-acetyltransferases 1 and 2.The Journal of pharmacology and experimental therapeutics · 2006Article
- N-acetyltransferase 2 genetic polymorphism: effects of carcinogen and haplotype on urinary bladder cancer risk.Oncogene · 2006Review
- Investigation of the catalytic triad of arylamine N-acetyltransferases: essential residues required for acetyl transfer to arylamines.The Biochemical journal · 2005Article
- Over-expression, purification, and characterization of recombinant human arylamine N-acetyltransferase 1.The protein journal · 2005Article
- Single-track sequencing for genotyping of multiple SNPs in the N-acetyltransferase 1 (NAT1) gene.BMC biotechnology · 2004Article
- Arylamine N-acetyltransferases: covalent modification and inactivation of hamster NAT1 by bromoacetamido derivatives of aniline and 2-aminofluorene.Journal of protein chemistry · 2003Article
- In silico analysis of potential inhibitors of Ca(2+) activated K(+) channel blocker, Charybdotoxin-C from Leiurus quinquestriatus hebraeus through molecular docking and dynamics studies.Indian journal of pharmacologyArticle
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arylamine N-acetyltransferases (EC 2.3.1.5) (NATs) catalyse the biotransformation of many primary arylamines, hydrazines and their N-hydroxylated metabolites, thereby playing an important role in both the detoxification and metabolic activation of numerous xenobiotics. The recently published crystal structure of the Salmonella typhimurium NAT (StNAT) revealed the existence of a cysteine protease-like (Cys-His-Asp) catalytic triad. In the present study, a three-dimensional homology model of human NAT1, based upon the crystal structure of StNAT [Sinclair, Sandy, Delgoda, Sim and Noble (2000) Nat. Struct. Biol. 7, 560-564], is demonstrated. Alignment of StNAT and NAT1, together with secondary structure predictions, have defined a consensus region (residues 29-131) in which 37% of the residues are conserved. Homology modelling provided a good quality model of the corresponding region in human NAT1. The location of the catalytic triad was found to be identical in StNAT and NAT1. Comparison of active-site structural elements revealed that a similar length loop is conserved in both species (residues 122-131 in NAT1 model and residues 122-133 in StNAT). This observation may explain the involvement of residues 125, 127 and 129 in human NAT substrate selectivity. Our model, and the fact that cysteine protease inhibitors do not affect the activity of NAT1, suggests that human NATs may have adapted a common catalytic mechanism from cysteine proteases to accommodate it for acetyl-transfer reactions.
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