Sulfotransferase family 1A member 1 (SULT1A1) (SULT1A1)

Sulfotransferase family 1A member 1 (SULT1A1) is a key cytosolic enzyme involved in the Phase II metabolism of various endogenous and exogenous compounds [1, 7]. It is highly expressed in the liver, gut, and hair follicles, where it catalyzes the transfer of a sulfate group from the donor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to substrates containing hydroxyl or amine groups [7, 9]. While this process generally facilitates the detoxification and elimination of compounds like estrogens and phenolic drugs, it also plays a crucial role in the bioactivation of certain pro-drugs, such as minoxidil, and the metabolic activation of environmental pro-carcinogens into reactive DNA-binding species [1, 2, 13]. Genetic polymorphisms, particularly the SULT1A1*2 (Arg213His) variant, lead to significant inter-individual differences in enzyme activity and thermal stability, which are linked to varying risks of cancer and inconsistent responses to medications like tamoxifen [3, 6, 11]. In dermatology, SULT1A1 activity in hair follicles is utilized as a biomarker to predict patient response to topical minoxidil for androgenetic alopecia [8, 10, 12]. Understanding SULT1A1's function is essential for optimizing drug therapy and assessing toxicological risks associated with environmental exposures [11, 14].

Other names

Phenol sulfotransferaseAryl sulfotransferase 1P-PSTSTPSTP1HAST1HAST2ST1A1ST1A3Thermostable phenol sulfotransferase 1

SULT1A1 catalyzes the transfer of a sulfate group from the universal donor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the hydroxyl or amine groups of various acceptor molecules [7, 9]. This sulfation reaction typically increases the water solubility and facilitates the renal excretion of drugs and hormones, but it can also bioactivate pro-drugs (e.g., minoxidil) or pro-carcinogens (e.g., N-hydroxyarylamines) into active or reactive metabolites [1, 2, 13].