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- Author
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Takuyu, Hashiguchi, Katsuhisa, Kurogi, Takehiko, Shimohira, Takamasa, Teramoto, Ming-Cheh, Liu, Masahito, Suiko, and Yoichi, Sakakibara
- Subjects
Cytosol ,Dehydroepiandrosterone Sulfate ,polycyclic compounds ,Androstenedione ,Humans ,Sulfotransferases ,Ketosteroids ,hormones, hormone substitutes, and hormone antagonists ,Mass Spectrometry ,Progesterone ,Article ,Protein Binding ,Substrate Specificity - Abstract
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.
- Published
- 2017