Results 151 to 160 of about 2,402 (195)
Allosteric regulation of arylamine N-acetyltransferase 1 by adenosine triphosphate [PDF]
Biochemical Pharmacology, 2018 In the present study, a screen of adenosine analogs as potential modulators of arylamine-N-acetyltransferase 1 activity identified ATP as an inhibitor within its range of physiological concentrations. Kinetically, ATP was a non-competitive inhibitor with
Neville Butcher +2 more
exaly +2 more sources
Design, synthesis and structure–activity relationships of 3,5-diaryl-1H-pyrazoles as inhibitors of arylamine N-acetyltransferase [PDF]
Bioorganic and Medicinal Chemistry Letters, 2013 The synthesis and inhibitory potencies of a novel series of 3,5-diaryl-1H-pyrazoles as specific inhibitors of prokaryotic arylamine N-acetyltransferase enzymes is described.
Elizabeth Fullam +2 more
exaly +2 more sources
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Expert Opinion on Drug Metabolism & Toxicology, 2007
Arylamine N-acetyltransferases (NATs), known as drug- and carcinogen-metabolising enzymes, have had historic roles in cellular metabolism, carcinogenesis and pharmacogenetics, including epidemiological studies of disease susceptibility. NAT research in the past 5 years builds on that history and additionally paves the way for establishing the following
Edith, Sim +2 more
openaire +3 more sources
Arylamine N-acetyltransferases (NATs), known as drug- and carcinogen-metabolising enzymes, have had historic roles in cellular metabolism, carcinogenesis and pharmacogenetics, including epidemiological studies of disease susceptibility. NAT research in the past 5 years builds on that history and additionally paves the way for establishing the following
Edith, Sim +2 more
openaire +3 more sources
Regulation of Arylamine N-Acetyltransferases
Current Drug Metabolism, 2008Acetylation catalysed by the arylamine N-acetyltransferases (NATs; 2.3.1.5) is a major biotransformation pathway for arylamine and hydrazine drugs, as well as many carcinogens that we are exposed to on a daily basis. These compounds can either be detoxified by NATs or bioactivated to metabolites that have the potential to cause toxicity such as cancer.
Butcher, Neville J. +2 more
openaire +5 more sources
Pharmacogenetics of the Human Arylamine N-Acetyltransferases
Pharmacology, 2000This review briefly describes current understanding of one of the earliest discovered pharmacogenetic polymorphisms of drug biotransformation affecting acetylation of certain homo- and heterocyclic aromatic amines and hydrazines. This so-called acetylation polymorphism arises from allelic variation in one of the two known human arylamine N ...
D M, Grant +3 more
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Arylamine N-acetyltransferases: From Structure to Function
Drug Metabolism Reviews, 2008Arylamine N-acetyltransferases (NATs) are cytosolic conjugating enzymes which transfer an acetyl group from acetylCoenzyme A to a xenobiotic acceptor substrate. The enzyme has an active site cysteine as part of a catalytic triad with histidine and aspartate. NATs have had an important role in pharmacogenetics.
Edith, Sim +2 more
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Structures of Human Arylamine N-Acetyltransferases
Current Drug Metabolism, 2008A large body of biochemical, kinetic and molecular information, accumulated over the course of more than 80 years, has produced valuable insights into the relationship between the structures and the catalytic functions of the human arylamine N-acetyltransferases NAT1 and NAT2.
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The Characteristics of Arylamine N-Acetyltransferase in Pseudomonas aeruginosa
Current Microbiology, 1998N-Acetyltransferase (NAT), responsible for bioactivation and detoxification of arylamines, has been demonstrated to be widely distributed in many organisms ranging from humans to microorganisms. Using high performance liquid chromatography (HPLC) to analyze NAT activity in bacteria, the authors found that Pseudomonas aeruginosa exhibited high NAT ...
S E, Hsieh, H H, Lo, J G, Chung
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Arylamine N-acetyltransferase Aggregation and Constitutive Ubiquitylation
Journal of Molecular Biology, 2006Arylamine N-acetyltransferases (NAT1 and NAT2) acetylate and detoxify arylamine carcinogens. Humans harboring certain genetic variations within the NAT genes exhibit increased likelihood of developing various cancer types, especially urinary bladder cancer.
Fen, Liu +6 more
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Arylamine N-acetyltransferases and Drug Response
Pharmacogenomics, 2002Arylamine N-acetyltransferases (NATs) play an important role in the interaction of competing metabolic pathways determining the fate of and response to xenobiotics as therapeutic drugs, occupational chemicals and carcinogenic substances. Individual susceptibility for drug response and possible adverse drug reactions are modulated by the genetic ...
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