ArticleThe Biochemical journal2005
Investigation of the catalytic triad of arylamine N-acetyltransferases: essential residues required for acetyl transfer to arylamines.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 61 citations in OpenAlex.
- Comparative Investigation of 15 Xenobiotic-MetabolizingApplied and environmental microbiology · 2021Article
- PtmC Catalyzes the Final Step of Thioplatensimycin, Thioplatencin, and Thioplatensilin Biosynthesis and Expands the Scope of ArylamineACS chemical biology · 2021Article
- Discovery of a previously unknown biosynthetic capacity of naringenin chalcone synthase by heterologous expression of a tomato gene cluster in yeast.Science advances · 2020Article
- Biochemical Characterization of ArylamineFrontiers in microbiology · 2020Article
- The actinobacterium Tsukamurella paurometabola has a functionally divergent arylamine N-acetyltransferase (NAT) homolog.World journal of microbiology & biotechnology · 2019Article
- A low-barrier hydrogen bond mediates antibiotic resistance in a noncanonical catalytic triad.Science advances · 2018Article
- Arylamine N-acetyltransferases: from drug metabolism and pharmacogenetics to drug discovery.British journal of pharmacology · 2014Review
- 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
- Arylamine N-acetyltransferases: a structural perspective.British journal of pharmacology · 2013Review
- Interaction of wild type, G68R and L125M isoforms of the arylamine-N-acetyltransferase from Mycobacterium tuberculosis with isoniazid: a computational study on a new possible mechanism of resistance.Journal of molecular modeling · 2012Article
- Purification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3].Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Understanding Protein Palmitoylation: Biological Significance and Enzymology.Science China. Chemistry · 2011Article
- Reaction mechanism of azoreductases suggests convergent evolution with quinone oxidoreductases.Protein & cell · 2010Article
- Probing the architecture of the Mycobacterium marinum arylamine N-acetyltransferase active site.Protein & cell · 2010Article
- Probing the catalytic potential of the hamster arylamine N-acetyltransferase 2 catalytic triad by site-directed mutagenesis of the proximal conserved residue, Tyr190.The FEBS journal · 2009Article
- Comparison of the Arylamine N-acetyltransferase from Mycobacterium marinum and Mycobacterium tuberculosis.The protein journal · 2009Article
- N-acetyltransferase SNPs: emerging concepts serve as a paradigm for understanding complexities of personalized medicine.Expert opinion on drug metabolism & toxicology · 2009Review
- Kinetic and chemical mechanism of arylamine N-acetyltransferase from Mycobacterium tuberculosis.Biochemistry · 2008Article
- Arylamine N-acetyltransferases in mycobacteria.Current drug metabolism · 2008Review
- Structure/function evaluations of single nucleotide polymorphisms in human N-acetyltransferase 2.Current drug metabolism · 2008Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 2 countries.
Funding
Abstract
The NATs (arylamine N-acetyltransferases) are a well documented family of enzymes found in both prokaryotes and eukaryotes. NATs are responsible for the acetylation of a range of arylamine, arylhydrazine and hydrazine compounds. We present here an investigation into the catalytic triad of residues (Cys-His-Asp) and other structural features of NATs using a variety of methods, including site-directed mutagenesis, X-ray crystallography and bioinformatics analysis, in order to investigate whether each of the residues of the catalytic triad is essential for catalytic activity. The catalytic triad of residues, Cys-His-Asp, is a well defined motif present in several families of enzymes. We mutated each of the catalytic residues in turn to investigate the role they play in catalysis. We also mutated a key residue, Gly126, implicated in acetyl-CoA binding, to examine the effects on acetylation activity. In addition, we have solved the structure of a C70Q mutant of Mycobacterium smegmatis NAT to a resolution of 1.45 A (where 1 A=0.1 nm). This structure confirms that the mutated protein is correctly folded, and provides a structural model for an acetylated NAT intermediate. Our bioinformatics investigation analysed the extent of sequence conservation between all eukaryotic and prokaryotic NAT enzymes for which sequence data are available. This revealed several new sequences, not yet reported, of NAT paralogues. Together, these studies have provided insight into the fundamental core of NAT enzymes, and the regions where sequence differences account for the functional diversity of this family. We have confirmed that each of the three residues of the triad is essential for acetylation activity.
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