Sulfotransferase 1A2 (SULT1A2)

Sulfotransferase 1A2 (SULT1A2) is a cytosolic enzyme belonging to the family of phenol-preferring sulfotransferases responsible for the sulfate conjugation of numerous hormones, neurotransmitters, drugs, and xenobiotic compounds[1][3][5][7]. SULT1A2 utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as a sulfonate donor, catalyzing the transfer of a sulfate group to phenolic substrates, which increases their water solubility and promotes their excretion[3][5][7]. The enzyme exhibits thermostable activity and is characterized by tissue- and substrate-specific expression patterns[1][3]. SULT1A2 is involved in both the detoxification and bioactivation of various substances, including certain carcinogens and active drug metabolites such as those of tamoxifen[3][4]. Recent studies suggest that SULT1A2 expression is elevated in bladder cancer, where it may serve as a prognostic marker for tumor staging and overall survival outcomes[2]. Genetic variants can alter enzyme activity, impacting the metabolism of therapeutic drugs (notably tamoxifen) and susceptibility to certain diseases[4][6]. SULT1A2 has also been implicated in metabolic conditions such as obesity and dyslipidemia[6]. The gene is generally not associated with a direct risk for major cancers other than as a modulator in specific tumor types (particularly bladder cancer)[2][3]. No spelling errors or evidence of the target being a pseudogene were detected in current biomedical usage; SULT1A2 is an established, validated molecular target[1][3][7].

Other names

ST1A2STP2P-PST 2HAST4Aryl sulfotransferase 2Phenol sulfotransferase 2Phenol-sulfating phenol sulfotransferase 2TSPST2P-PST

Sulfate conjugation (sulfation) of drugs and hormones, increasing their solubility and facilitating excretion; Metabolic activation of procarcinogens by sulfonation of N-hydroxyarylamines, leading to DNA adducts; Modulation of drug efficacy and toxicity by altering active metabolite levels