Results 191 to 200 of about 17,285 (228)

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   +4 more sources

Arylamine N-acetyltransferase I

The International Journal of Biochemistry & Cell Biology, 2007
Arylamine N-acetyltransferase I (NAT1) is a phase II enzyme that acetylates a wide range of arylamine and hydrazine substrates. The NAT1 gene is located on chromosome 8 and shares homology to NAT genes found in most mammalian species. Gene expression occurs from at least two promoters and a number of tissue-specific transcripts have been identified ...
Minchin, RF, Hanna, PE, Dupret, JM, Wagner, CR, Rodrigues-Lima, F, Butcher, NJ   +5 more
openaire   +4 more sources

Identification and Characterization of Functional Rat Arylamine N-Acetyltransferase 3: Comparisons with Rat Arylamine N-Acetyltransferases 1 and 2 [PDF]

The Journal of Pharmacology and Experimental Therapeutics, 2006
Arylamine N-acetyltransferases (NATs; EC 2.3.1.5) catalyze both the N-acetylation and O-acetylation of arylamines and N-hydroxyarylamines. Humans possess two functional N-acetyltransferase genes, NAT1 and NAT2, as well as a nonfunctional pseudogene, NATP. Previous studies have identified Nat1 and Nat2 genes in the rat.
Jason M. Walraven, Mark A. Doll, David W. Hein   +2 more
openaire   +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 ...
Denis M. Grant, Geoffrey H. Goodfellow, Kim S. Sugamori, Kristi Durette   +3 more
openaire   +2 more sources

Arylamine N-acetyltransferases: From Structure to Function

Drug Metabolism Reviews, 2008
Arylamine 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.
Sotiria Boukouvala, Edith Sim, Kylie J. Walters   +2 more
openaire   +2 more sources

Small Molecule Inhibitors of Arylamine N-Acetyltransferase 1 Attenuate Cellular Respiration.

ACS Pharmacology & Translational Science
Arylamine N-acetyltransferase 1 (NAT1) expression has been shown to attenuate mitochondrial function, suggesting it is a promising drug target in diseases of mitochondrial dysfunction.
C. Choudhury, James E. Egleton, N. Butcher, Angela J. Russell, R. Minchin   +4 more
semanticscholar   +1 more source

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.
Kylie J. Walters, Fen Liu, Naixia Zhang, Deanna M. Koepp, Patrick E. Hanna, Xin Zhou, Carston R. Wagner   +6 more
openaire   +3 more sources

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 ...
Sue Er Hsieh, Hsueh Hsia Lo, Jing Gung Chung   +2 more
openaire   +3 more sources

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, Marta Martins, Fernando Rodrigues-Lima, Julien Dairou, Jean-Marie Dupret, Philippe Silar, Philippe Silar   +6 more
openaire   +3 more sources

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 ...
Nichola Johnson, Anna Upton, James Sandy, Edith Sim   +3 more
openaire   +3 more sources