SULT2A1 Protein, Human (His)

SULT2A1 protein, a sulfotransferase utilizing 3'-phospho-5'-adenylyl sulfate (PAPS) as its sulfonate donor, serves as a crucial mediator in the sulfonation of steroids and bile acids within the liver and adrenal glands. Demonstrating versatile enzymatic activity, SULT2A1 facilitates the sulfation of an extensive array of steroids and sterols, including pregnenolone, androsterone, DHEA, bile acids, cholesterol, and numerous xenobiotics featuring alcohol and phenol functional groups. This sulfonation process enhances the water solubility of these compounds, facilitating their renal excretion; however, it also has the potential to lead to bioactivation, forming active metabolites. SULT2A1's multifaceted roles extend to maintaining steroid and lipid homeostasis, playing a pivotal role in bile acid metabolism, and catalyzing the metabolic activation of potent carcinogenic polycyclic arylmethanols. The diverse substrate specificity of SULT2A1 underscores its significance in regulating essential physiological processes and its potential involvement in the metabolic activation of compounds with carcinogenic properties.