Results 201 to 210 of about 17,361 (234)

Molecular Docking and Pharmacokinetic Prediction Studies of Novel Coumarin Derivatives as Arylamine N- acetyltransferase 2 Inhibitors

Current Aspects in Pharmaceutical Research and Development Vol. 2, 2021
Arylamine N-acetyltransferases are xenobiotic-metabolizing enzymes responsible for detoxification of many drugs and carcinogens. It catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate ...
S. George, P. K. Sujith, M. Chandran, Kumaran Santhalingam   +3 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.
Fen, Liu, Naixia, Zhang, Xin, Zhou, Patrick E, Hanna, Carston R, Wagner, Deanna M, Koepp, Kylie J, Walters   +6 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.
Edith, Sim, Kylie, Walters, Sotiria, Boukouvala   +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 ...
D M, Grant, G H, Goodfellow, K, Sugamori, K, Durette   +3 more
openaire   +2 more sources

Arylamine N-acetyltransferase in human red blood cells

Biochemical Pharmacology, 1992
N-Acetyltransferase activities associated with erythrocytes from 20 individuals have been determined with p-aminobenzoic acid as substrate. A three-fold variation in Vmax is found. The N-acetyltransferase genotype of the individuals has been determined and there is no correlation between the extent of acetylation measured in the individuals ...
A, Ward, D, Hickman, J W, Gordon, E, Sim
openaire   +2 more sources

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.
openaire   +2 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 ...
A, Upton, N, Johnson, J, Sandy, E, Sim
openaire   +2 more sources

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 ...
openaire   +2 more sources

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

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

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
openaire   +2 more sources