Results 141 to 150 of about 13,476,144 (183)

Evidence for two closely related isozymes of arylamine N -acetyltransferase in human liver [PDF]

FEBS Letters, 1989
Acetyl CoA-dependent arylamine N-acetyltransferase (EC 2.3.1.5) is the target of a genetic polymorphism in the metabolism of drugs and carcinogens. N-Acetyltransferase was purified 1000-fold from cytosol of human liver and its identity was verified by ...
Denis Grant, Urs A Meyer
exaly   +2 more sources

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Regulation of Arylamine N-Acetyltransferases

Current Drug Metabolism, 2008
Acetylation 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., Tiang, Jacky, Minchin, Rodney F.   +2 more
openaire   +5 more sources

Design, synthesis and structure–activity relationships of 3,5-diaryl-1H-pyrazoles as inhibitors of arylamine N-acetyltransferase

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, Edith Sim, Steve Davies   +2 more
exaly   +2 more sources

Pharmacogenetics of the Human Arylamine N-Acetyltransferases

Pharmacology, 2000
This 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, G H, Goodfellow, K, Sugamori, K, Durette   +3 more
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Structures of Human Arylamine N-Acetyltransferases

Current Drug Metabolism, 2008
A 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, 1998
N-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, 2006
Arylamine 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, Naixia, Zhang, Xin, Zhou, Patrick E, Hanna, Carston R, Wagner, Deanna M, Koepp, Kylie J, Walters   +6 more
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Insights into the Phylogeny or Arylamine N-Acetyltransferases in Fungi

Journal of Molecular Evolution, 2010
Previous studies have shown that Eumycetes fungi can acylate arylamine thanks to arylamine N-acetyltransferases, xenobiotic-metabolizing enzymes also found in animals and bacteria. In this article, we present the results of mining 96 available fungal genome sequences for arylamine N-acetyltransferase genes and propose their phylogeny.
Marta, Martins, Julien, Dairou, Fernando, Rodrigues-Lima, Jean-Marie, Dupret, Philippe, Silar   +4 more
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Arylamine N-acetyltransferases and Drug Response

Pharmacogenomics, 2002
Arylamine 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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Arylamine N-acetyltransferases – of mice, men and microorganisms

Trends in Pharmacological Sciences, 2001
Arylamine N-acetyltransferases (NATs) catalyse the transfer of an acetyl group from acetyl CoA to the terminal nitrogen of hydrazine and arylamine drugs and carcinogens. These enzymes are polymorphic and have an important place in the history of pharmacogenetics, being first identified as responsible for the polymorphic inactivation of the anti ...
A, Upton, N, Johnson, J, Sandy, E, Sim
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