کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9002246 | 1118578 | 2005 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Eukaryotic arylamine N-acetyltransferase
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کلمات کلیدی
INH5AsDTTNATDTNBDLS5-aminosalicylate - 5-آمینوسالیات5,5′-dithio-bis(2-nitrobenzoic acid) - 5،5'-dithio-bis (2-nitrobenzoic acid)arylamine N-acetyltransferase - آریلامین N-استیل ترانسفرازArylamines - آریلامین هاisoniazid - ایزونیازیدdithiothreitol - دیتیوتریتولcircular dichroism - رنگ تابی دورانیXenobiotic metabolism - سوخت و ساز بدن Xenobiotichigh-throughput screening - غربالگری بالاIAM - من هستمHydralazine - هیدرازینPABA - پاباDynamic Light Scattering - پراکندگی نور دینامیکیRecombinant protein - پروتئین های نوترکیبiodoacetamide - یووداکتامید
موضوعات مرتبط
علوم پزشکی و سلامت
داروسازی، سم شناسی و علوم دارویی
داروشناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Arylamine N-acetyltransferases (NAT; EC 2.3.1.5) catalyse the transfer of acetyl groups from acetylCoA to xenobiotics, including drugs and carcinogens. The enzyme is found extensively in both eukaryotes and prokaryotes, yet the endogenous roles of NATs are still unclear. In order to study the properties of eukaryotic NATs, high-throughput substrate and inhibitor screens have been developed using pure soluble recombinant Syrian hamster NAT2 (shNAT2) protein. The assay can be used with a wide range of compounds and was used to determine substrate specificity of shNAT2. We describe the expression and characterisation of shNAT2 and also purified recombinant human NAT1 and NAT2, including the use of the assay to explore the substrate specificities of each of the enzymes. Hamster NAT2 has similar substrate specificity to human NAT1, acetylating para-aminobenzoate but not arylhydrazine and hydralazine compounds. The overlapping but distinct substrate-specific activity profiles of human NAT1 and NAT2 were clearly observed from the screen. Naturally occurring compounds were tested as substrates or inhibitors of shNAT2 and succinylCoA was found to be a potent inhibitor of shNAT2.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical Pharmacology - Volume 69, Issue 2, 15 January 2005, Pages 347-359
Journal: Biochemical Pharmacology - Volume 69, Issue 2, 15 January 2005, Pages 347-359
نویسندگان
Akane Kawamura, James Graham, Adeel Mushtaq, Stefanos A. Tsiftsoglou, Gregory M. Vath, Patrick E. Hanna, Carston R. Wagner, Edith Sim,