Δ4-3-ketosteroids as a new class of substrates for the cytosolic sulfotransferases

Takuyu Hashiguchi, Katsuhisa Kurogi, Takehiko Shimohira, Takamasa Teramoto, Ming Cheh Liu, Masahito Suiko, Yoichi Sakakibara

研究成果: Contribution to journalArticle査読

2 被引用数 (Scopus)

抄録

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 Δ4-3-ketosteroids, which carry no hydroxyl groups in their chemical structure. Among a panel of Δ4-3-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 Δ4-3-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 Δ4-3-ketosteroid sulfotransferase in steroid metabolism.

本文言語英語
ページ(範囲)2883-2890
ページ数8
ジャーナルBiochimica et Biophysica Acta - General Subjects
1861
11
DOI
出版ステータス出版済み - 11 2017

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学

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