Biochemical and Biophysical Research Communications
Regular Article3D Model of Human Arylamine N-Acetyltransferase 2: Structural Basis of the Slow Acetylator Phenotype of the R64Q Variant and Analysis of the Active-Site Loop☆
References (29)
- et al.
Arylamine N-acetyltransferases—Of mice, men and microorganisms
Trends Pharmacol. Sci.
(2001) - et al.
Site-directed mutagenesis of recombinant human arylamine N-acetyltransferase expressed in Escherichia coli. Evidence for direct involvement of Cys68 in the catalytic mechanism of polymorphic human NAT2
J. Biol. Chem.
(1992) - et al.
Involvement of Cys69 residue in the catalytic mechanism of N-hydroxyarylamine O-acetyltransferase of Salmonella typhimurium. Sequence similarity at the amino acid level suggests a common catalytic mechanism of acetyltransferase for S. typhimurium and higher organisms
J. Biol. Chem.
(1992) - et al.
Structure–function studies of human arylamine N-acetyltransferases NAT1 and NAT2. Functional analysis of recombinant NAT1/NAT2 chimeras expressed in Escherichia coli
J. Biol. Chem.
(1994) - et al.
BLAST 2 sequences, a new tool for comparing protein and nucleotide sequences
FEMS Microbiol. Lett.
(1999) Protein secondary structure prediction based on position-specific scoring matrices
J. Mol. Biol.
(1999)- et al.
Comparative protein modelling by satisfaction of spatial restraints
J. Mol. Biol.
(1993) The first 3D structure of arylamine N-acetyltransferase reveals a protease-like catalytic triad
Trends Pharmacol. Sci.
(2000)- et al.
Three-dimensional view of the surface motif associated with the P-loop structure: Cis and trans cases of convergent evolution
J. Mol. Biol.
(2000) - et al.
A fragment consisting of the first 204 amino-terminal amino acids of human arylamine N-acetyltransferase one (NAT1) and the first transacetylation step of catalysis
Biochem. Pharmacol.
(1997)
Mapping AAC1, AAC2 and AACP, the genes for arylamine N-acetyltransferases, carcinogen metabolising enzymes on human chromosome 8p22, a region frequently deleted in tumours
Cytogenet. Cell Genet.
Molecular genetics and epidemiology of the NAT1 and NAT2 acetylation polymorphisms
Cancer Epidemiol. Biomarkers Prev.
An update on genetic, structural and functional studies of arylamine N-acetyltransferases in eucaryotes and procaryotes [in process citation]
Hum. Mol. Genet.
Update on consensus arylamine N-acetyltransferase gene nomenclature [letter]
Pharmacogenetics
Cited by (49)
Review of NEDDylation inhibition activity detection methods
2021, Bioorganic and Medicinal ChemistryCitation Excerpt :The idea of molecular docking can be traced back to Fisher’s “lock and key” model in the 19th century.75 With the development of receptor theory, the understanding of the interaction between two molecules changed from the rigid model of spatial matching to the flexible model of spatial interaction and energy matching.76 In the process of computer simulation of drug design, molecular docking has gradually developed into an important method for compound screen.77
The role of lysine<sup>100</sup> in the binding of acetylcoenzyme A to human arylamine N-acetyltransferase 1: Implications for other acetyltransferases
2015, Biochemical PharmacologyCitation Excerpt :They are distinguished by the presence of a conserved catalytic triad that prefers aromatic amine and hydrazine substrates [2]. In humans, there are 2 NATs (NAT1 and NAT2) and their crystal structure and catalytic function have been described in detail [3–6]. Both NAT1 and NAT2 are genetically polymorphic, which impacts on the pharmacology of many therapeutic agents that are metabolized by these enzymes [7].
Sequence analysis of NAT2 gene in Brazilians: Identification of undescribed single nucleotide polymorphisms and molecular modeling of the N-acetyltransferase 2 protein structure
2010, Mutation Research - Fundamental and Molecular Mechanisms of MutagenesisMethods for Predicting Human Drug Metabolism
2007, Advances in Clinical ChemistryNMR-based Model Reveals the Structural Determinants of Mammalian Arylamine N-Acetyltransferase Substrate Specificity
2006, Journal of Molecular Biology
- ☆
Abbreviations used: Ac-CoA, acetyl-CoA; NAT, arylamine N-acetyltransferase; rmsd, root mean square deviation.
- 1
To whom correspondence and reprint requests should be addressed at CNRS UMR 7000, Faculté de Médecine Pitié-Salpêtrière, 105 Bd de l'Hôpital, 75013 Paris, France. Fax: (33 1) 53 60 08 02. E-mail: [email protected].