Sulfotransferase 1A1 (SULT1A1)

Sulfotransferase 1A1 (SULT1A1) is a cytosolic enzyme highly expressed in the human liver and other tissues, catalyzing the sulfonation (sulfate conjugation) of a wide variety of endogenous compounds, including steroid hormones, neurotransmitters, and phenolic drugs, as well as xenobiotic toxins[2][4][5][6]. SULT1A1 uses 3′-phosphoadenosine 5′-phosphosulfate (PAPS) as a sulfate donor to modify substrates, generally increasing their water solubility for renal excretion[2][4]. The enzyme displays exceptionally broad substrate specificity, facilitated by a structurally flexible active site, and is dynamically regulated by both nucleotide (PAPS) binding and allosteric modulation[1][3][5]. SULT1A1 activity is clinically important in drug metabolism and detoxification as well as hormone regulation, and it serves as a pharmacogenetic determinant in responses to medications such as minoxidil (for hair growth disorders), where its expression in hair follicles predicts therapeutic efficacy[6]. Variability in SULT1A1 function can contribute to differences in drug metabolism, efficacy, and toxicity among individuals[6].

Other names

Aryl sulfotransferase 1HAST1HAST2P-PST 1Phenol sulfotransferase 1Phenol-sulfating phenol sulfotransferase 1ST1A1ST1A3STPSTP1Thermostable phenol sulfotransferaseTs-PST

Sulfonation: transfer of a sulfuryl group (–SO3) from the donor 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to hydroxyl or amine groups of substrates, increasing solubility and enhancing renal excretion or forming active metabolites[2][4][5] Bioactivation (in some cases, conversion of inactive to active drugs, e.g., minoxidil to minoxidil sulfate in hair follicles)[6]