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

Biochim Biophys Acta Gen Subj. 2017 Nov;1861(11 Pt A):2883-2890. Epub 2017 Aug 03
Takuyu Hashiguchi 1 , Katsuhisa Kurogi 1 , Takehiko Shimohira 1 , Takamasa Teramoto 2 , Ming-Cheh Liu 3 , Masahito Suiko 1 , Yoichi Sakakibara 4
Takuyu Hashiguchi 1 , Katsuhisa Kurogi 1 , Takehiko Shimohira 1 , Takamasa Teramoto 2 , Ming-Cheh Liu 3 , Masahito Suiko 1 , Yoichi Sakakibara 4
+ et al

[No authors listed]

Author information
  • 1 Department of Biochemistry and Applied Biosciences, University of Miyazaki, Miyazaki, Miyazaki 889-2192, Japan; Interdisciplinary Graduate School of Agriculture and Engineering, University of Miyazaki, Miyazaki, Miyazaki 889-2192, Japan.
  • 2 Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University, Hakozaki 6-10-1, Fukuoka 812-8581, Japan.
  • 3 Department of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, Toledo, OH 43614, USA.
  • 4 Department of Biochemistry and Applied Biosciences, University of Miyazaki, Miyazaki, Miyazaki 889-2192, Japan; Interdisciplinary Graduate School of Agriculture and Engineering, University of Miyazaki, Miyazaki, Miyazaki 889-2192, Japan. Electronic address: ysakaki@cc.miyazaki-u.ac.jp.

摘要


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.

KEYWORDS: 4-androstene-3,17-dione, Ketosteroid, Ketosteroid isomerase, Sulfotransferase