2017年11月
Δ4-3-ketosteroids as a new class of substrates for the cytosolic sulfotransferases
Biochimica et Biophysica Acta - General Subjects
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- 巻
- 1861
- 号
- 11
- 開始ページ
- 2883
- 終了ページ
- 2890
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bbagen.2017.08.005
- 出版者・発行元
- Biochimica et Biophysica Acta - General Subjects
© 2017 Elsevier B.V. Cytosolic sulfotransferase (SULT)-mediated sulfation is generally known to involve the transfer of a sulfonate group from the active sulfate, 3′-phosphoadenosine 5′-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 Δ 4 -3-ketosteroids, which carry no hydroxyl groups in their chemical structure. Among a panel of Δ 4 -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 Δ 4 -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 Δ 4 -3-ketosteroid sulfotransferase in steroid metabolism.
- リンク情報
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- DOI
- https://doi.org/10.1016/j.bbagen.2017.08.005
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000415768500037&DestApp=WOS_CPL
- URL
- https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85027727007&origin=inward
- ID情報
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- DOI : 10.1016/j.bbagen.2017.08.005
- ISSN : 0304-4165
- eISSN : 1872-8006
- Web of Science ID : WOS:000415768500037