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Acetylation of aromatic cysteine conjugates by recombinant humanN-acetyltransferase 8

التفاصيل البيبلوغرافية
العنوان: Acetylation of aromatic cysteine conjugates by recombinant humanN-acetyltransferase 8
المؤلفون: P. David Josephy, Reema Deol
المصدر: Xenobiotica. 47:202-207
بيانات النشر: Informa UK Limited, 2016.
سنة النشر: 2016
مصطلحات موضوعية: 0301 basic medicine, Stereochemistry, Health, Toxicology and Mutagenesis, N-acetyltransferase, Toxicology, Biochemistry, law.invention, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Acetyltransferases, law, Humans, Cysteine, Mercapturic acid, Pharmacology, chemistry.chemical_classification, Acetylation, General Medicine, Glutathione, HEK293 Cells, 030104 developmental biology, Enzyme, chemistry, 030220 oncology & carcinogenesis, Recombinant DNA, Conjugate
الوصف: 1. The mercapturic acid (MA) pathway is a metabolic route for the processing of glutathione conjugates to MA (N-acetylcysteine conjugates). An N-acetyltransferase enzyme, NAT8, catalyzes the transfer of an acetyl group from acetyl-CoA to the cysteine amino group, producing a MA, which is excreted in the urine. We expressed human NAT8 in HEK293T cells and developed an HPLC-MS method for the quantitation of the S-aryl-substituted cysteine conjugates and their MA.2. We measured the activity of the enzyme for acetylation of benzyl-, 4-nitrobenzyl-, and 1-menaphthylcysteine substrates.3. NAT8 catalyzed the acetylation of all three cysteine conjugates with similar Michaelis–Menten kinetics.
تدمد: 1366-5928
0049-8254
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83ff9bacfcc00041521a52bad0382f20
https://doi.org/10.1080/00498254.2016.1178410
رقم الأكسشن: edsair.doi.dedup.....83ff9bacfcc00041521a52bad0382f20
قاعدة البيانات: OpenAIRE
الوصف
تدمد:13665928
00498254