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

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

SUBMITTER: Hashiguchi T 

PROVIDER: S-EPMC5623657 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature