Steroid sulfotransferase (SULT (or SULTs for the family))

Steroid sulfotransferase refers to a subfamily of cytosolic enzymes that catalyze the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to steroid hormones, drugs, neurotransmitters, and other small molecules (a reaction known as sulfonation or sulfate conjugation)[3][4][5][6]. These enzymes, particularly types such as SULT1A1 and SULT2A1, play essential roles in regulating the biological activity of steroids (by converting them to inactive sulfated forms), as well as in detoxification and the metabolism of a wide array of endogenous and xenobiotic compounds[4][5][6]. Sulfonation generally increases water solubility and promotes clearance, but certain SULT-mediated reactions may bioactivate procarcinogens. These enzymes show tissue-specific expression and considerable genetic variation, which can influence drug metabolism and disease risk[4][5]. SULT1A1, for example, is important in the activation of minoxidil, a treatment for hair loss, where its activity level can predict patient response[5].\n\nCaveat: "Steroid sulfotransferase" is a functional class encompassing several specific enzymes (e.g., SULT1A1, SULT2A1). Where possible, research may need to specify the precise isoform.

Other names

SULTSULT1A1SULT2A1phenol sulfotransferasecytosolic sulfotransferaseestrogen sulfotransferase

Catalyzes the transfer of a sulfate group from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to hydroxyl groups of target molecules, producing sulfate-conjugated metabolites