This letter is a comment on Zhou . (2013). Arylamine N-acetyltransferases: a structural perspective. Br J Pharmacol 169: 748–760. To view this article visit http://dx.doi.org/10.1111/bph.12182
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The Arylamine N-Acetyltransferases as Therapeutic Targets in Metabolic Diseases Associated with Mitochondrial Dysfunction.
Pharmacol Rev
February 2024
School of Biomedical Sciences (C.C., M.K.G., C.E.M., N.J.B., F.J.S., R.F.M.) and Australian Institute for Bioengineering and Nanotechnology (S.T.N.), University of Queensland, Brisbane, Australia.
In humans, there are two arylamine N-acetyltransferase genes that encode functional enzymes ( and ) as well as one pseudogene, all of which are located together on chromosome 8. Although they were first identified by their role in the acetylation of drugs and other xenobiotics, recent studies have shown strong associations for both enzymes in a variety of diseases, including cancer, cardiovascular disease, and diabetes. There is growing evidence that this association may be causal.
View Article and Find Full Text PDFContrasting Effects of Temperature on Human Arylamine -Acetyltransferase and Acetyl Coenzyme A Hydrolase Activities.
Biochemistry
July 2023
School of Biomedical Sciences, The University of Queensland, St. Lucia, Queensland 4072, Australia.
There are two human arylamine -acetyltransferases (NAT1 and NAT2) that have evolved separately and differ in their substrate specificity and tissue localization. In addition to its acetyltransferase activity, NAT1 can hydrolyze acetyl coenzyme A to coenzyme A in the presence of folate. Here, we show that NAT1 is rapidly inactivated at temperatures above 39 °C whereas NAT2 is more stable.
View Article and Find Full Text PDFAltered Arylamine N-acetyltransferase 1 and miR-1290 Levels in Childhood Acute Lymphoblastic Leukemia: A Pilot Study.
In Vivo
May 2023
Faculty of Chemical Sciences, Autonomous University of San Luis Potosí, San Luis Potosi, SLP, Mexico;
Background/aim: Arylamine N-acetyltransferase 1 and 2 (NAT1 and NAT2) are drug-metabolizing enzymes that play a key role in the development of acute lymphoblastic leukemia (ALL).
Materials And Methods: This study evaluated NAT1 and NAT2 mRNA and protein expression and their enzymatic activity in peripheral blood mononuclear cells (PBMC) from patients with ALL (n=20) and healthy children (n=19) and explored the mechanisms that regulate these enzymes in ALL such as microRNAs (miR-1290, miR-26b) and SNPs.
Results: PBMC from patients with ALL showed a decrease in NAT1 mRNA and protein expression.
Function, structure, evolution, regulation of a potent drug target, arylalkylamine N-acetyltransferase.
Adv Protein Chem Struct Biol
March 2023
Laboratory of Tropical Veterinary Medicine and Vector Biology, School of Life Sciences, Hainan University, Haikou, Hainan, P.R. China; One Health Institute, Hainan University, Haikou, Hainan, P.R. China. Electronic address:
Arylalkylamine N-acetyltransferase (aaNAT) catalyzes the transacetylation of acetyl coenzyme A to arylamines and arylalkylamines. Based on three-dimensional structural information, aaNAT belongs to the GCN5-related N-acetyltransferases superfamily with a conserved acetyl-CoA binding domain (Dyda et al., 2000).
View Article and Find Full Text PDFMolecular and Functional Characterization of -Acetyltransferases in Common Marmosets and Pigs.
Drug Metab Dispos
November 2022
Joint Faculty of Veterinary Medicine, Kagoshima University, Kagoshima, Japan (Y.U., M.I., A.A., M.S.); Laboratory of Drug Metabolism and Pharmacokinetics, Showa Pharmaceutical University, Tokyo, Japan(S.U., K.B., N.M., H.Y.); and School of Veterinary Medicine, Kitasato University, Aomori, Japan (H.K.)
Arylamine -acetyltransferases (NATs) are drug-metabolizing enzymes that are essential for the metabolism of endogenous substrates and xenobiotics. The molecular characteristics of NATs have been extensively investigated in humans but remain to be investigated in common marmosets and pigs, animal species that are often used in drug metabolism studies. In this study, marmoset NAT1 and pig NAT1 cDNAs were isolated from liver samples and were characterized by molecular analyses and drug-metabolism assays.
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