کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5507878 | 1537481 | 2017 | 42 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Î4-3-ketosteroids as a new class of substrates for the cytosolic sulfotransferases
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Cytosolic sulfotransferase (SULT)-mediated sulfation is generally known to involve the transfer of a sulfonate group from the active sulfate, 3â²-phosphoadenosine 5â²-phosphosulfate (PAPS), to a hydroxyl group or an amino group of a substrate compound. We report here that human SULT2A1, in addition to being able to sulfate dehydroepiandrosterone (DHEA) and other hydroxysteroids, could also catalyze the sulfation of Î4-3-ketosteroids, which carry no hydroxyl groups in their chemical structure. Among a panel of Î4-3-ketosteroids tested as substrates, 4-androstene-3,17-dione and progesterone were found to be sulfated by SULT2A1. Mass spectrometry analysis and structural modeling supported a reaction mechanism which involves the isomerization of Î4-3-ketosteroids from the keto form to an enol form, prior to being subjected to sulfation. Results derived from this study suggested a potential role of SULT2A1 as a Î4-3-ketosteroid sulfotransferase in steroid metabolism.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1861, Issue 11, Part A, November 2017, Pages 2883-2890
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1861, Issue 11, Part A, November 2017, Pages 2883-2890
نویسندگان
Takuyu Hashiguchi, Katsuhisa Kurogi, Takehiko Shimohira, Takamasa Teramoto, Ming-Cheh Liu, Masahito Suiko, Yoichi Sakakibara,