Sulfotransferase (SULT) (SULT)

Sulfotransferases (SULTs) are a superfamily of enzymes that play a pivotal role in the Phase II metabolism of both endogenous molecules and exogenous compounds, including drugs and environmental toxins (Falany, 1997, FASEB J). These enzymes catalyze the transfer of a sulfonate group from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to substrate molecules, typically increasing their water solubility and facilitating renal excretion (Coughtrie, 2016, Drug Metab Dispos). While often considered a detoxification pathway, sulfonation can also bioactivate certain compounds into highly reactive electrophiles, contributing to chemical carcinogenesis and drug-induced toxicity (Gamage et al., 2006, Toxicol Sci). SULTs are essential for regulating the biological activity of steroid hormones, thyroid hormones, and catecholamine neurotransmitters by modulating their receptor binding affinity (Negishi et al., 2001, Arch Biochem Biophys). In the context of pharmacology, SULTs are significant due to their involvement in the metabolism of drugs like tamoxifen and acetaminophen, where genetic variations in SULT isoforms can lead to inter-individual differences in drug response and safety profiles (Hildebrandt et al., 2007, Pharmacogenet Genomics).

Other names

Sulfotransferase familyCytosolic sulfotransferaseMembrane-bound sulfotransferaseSTSulfotransferase enzyme

Sulfotransferases catalyze the transfer of a sulfonate group from the universal donor 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to the hydroxyl or amino groups of various substrates, a process known as sulfonation or sulfation (Coughtrie, 2016, Drug Metab Dispos).