Results 201 to 210 of about 17,285 (228)

Arylamine N-Acetyltransferases

2018
Arylamine N-acetyltransferases (NATs) are cytosolic conjugating enzymes that add an acetyl group from acetyl coenzyme A (CoA) to arylamine and arylhydrazines that in general are detoxification reactions. Acetylation of arylhydroxylamines and the transfer of an acetyl group from the O to N group of arylacetohydroxates generally result in activation ...
N. Laurieri, E. Sim, E. Polycarpou
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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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Arylamine N‐Acetyltransferase in Erythrocytes of Cystic Fibrosis Patients

Pharmacology & Toxicology, 1996
Abstract:Sulphamethoxazole, a substrate of human arylamine N‐acetyltransferase, is used in the treatment of cystic fibrosis patients, who metabolise the drug rapidly. Increased metabolic clearance of sulphamethoxazole has been suggested to account for this rapid metabolism.
A Ward, D Lane, Valerie Smelt, W van der Slot, Edith Sim, Angela Risch, Lesley A. Stanley   +6 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-acetyltransferase activity of the human placenta.

The Journal of Pharmacology and Experimental Therapeutics, 1994
The fetus is exposed to almost all of the substances found in the maternal circulation whether nutrients or foreign chemicals ("xenobiotics"). The main route of exposure is the placenta. The placenta is metabolically active toward xenobiotics and the nature of the compounds reaching the fetal circulation will, in part, depend on placental ...
L O, Derewlany, B, Knie, G, Koren
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Identification of arylamine N-acetyltransferase activity in the bovine lens

Current Eye Research, 1995
Arylamine N-acetyltransferase (NAT) activity was identified and partially characterized in the bovine lens. According to size-exclusion HPLC, the molecular mass of the arylamine NAT is approximately 30-kDa. Based upon substrate specificity analysis, it is best described as an arylamine NAT which has some ability to N-acetylate arylalkylamines.
Pouneh Razavi, Gerald J. Chader, Stephen J. Gaudet, Guy J. Caiafa   +3 more
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Interaction of Human Arylamine N-Acetyltransferase 1 with Different Nanomaterials [PDF]

Drug Metabolism and Disposition, 2014
Humans are exposed to nanoparticles in the environment as well as those in nanomaterials developed for biomedical applications. However, the safety and biologic effects of many nanoparticles remain to be elucidated. Over the past decade, our understanding of the interaction of proteins with various nanomaterials has grown.
Deng, Zhou J., Butcher, Neville J., Mortimer, Gysell M., Jia, Zhongfan, Monteiro, Michael J., Martin, Darren J., Minchin, Rodney F.   +6 more
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Human arylamine N-acetyltransferase genes: isolation, chromosomal localization, and functional expression.

DNA and Cell Biology, 1990
N-Acetylation by hepatic arylamine N-acetyltransferase (NAT, EC 2.3.1.5) is a major route in the metabolism and detoxification of numerous drugs and foreign chemicals.
M. Blum, D. Grant, W. Mcbride, M. Heim, U. Meyer   +4 more
semanticscholar   +1 more source

Evidence for Arylamine N-Acetyltransferase Activity in the Escherichia coli

Current Microbiology, 1998
N-Acetyltransferase activities with p-aminobenzoic acid and 2-aminofluorene as substrates were determined in isolates of the bacterium Escherichia coli. The N-acetyltransferase activity was determined by an acetyl CoA recycling assay and high pressure liquid chromatography. The N-acetyltransferase activities from a number of E. coli isolates were found
Jing-Gung Chung, Fang C. Chang
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Arylamine N-acetyltransferase (NAT2) genotypes in a Turkish population

Pharmacogenetics, 1997
A group of 303 unrelated Turkish subjects from south-east Anatolia was genotyped for seven NAT2 mutations by polymerase chain reaction-restriction fragment length polymorphism. Genotypes associated with slow acetylation were identified in 57.4% (95%-confidence limits, 51.6%-63.1%).
Przemyslaw M. Mrozikiewicz, Ingolf Cascorbi, A S Aynacioglu, Ivar Roots   +3 more
openaire   +3 more sources