The identity of alcohol sulfotransferases with hydroxysteroid sulfotransferases

Ethanol Sulfation by the Human Cytosolic Sulfotransferases: A Systematic Analysis

“…16) These latter results, however, might have been affected by undetermined levels of the expression of different SULTs in S. typhimurium cells and/or the inhibitory/stimulatory effects of compounds present in the crude cell homogenates used as the source of the SULT enzyme(s) in the assay for sulfation of ethanol. It is noted that SULT2A1, while previously referred to as alcohol sulfotransferase, 32) displayed much lower ethanol-sulfating activity than did members of the phenol sulfotransferase family including SULT1A1, SULT1A2, SULT1A3, and SULT1C4. While the rationale for the low ethanol-sulfating activity of SULT2A1 remains to be clarified, previous studies have demonstrated that SULT2A1 displayed much lower activity and affinity toward ethanol than other alcohols including butanol, hexanol, cyclohexylmethanol, and benzyl alcohol.…”

“…While the rationale for the low ethanol-sulfating activity of SULT2A1 remains to be clarified, previous studies have demonstrated that SULT2A1 displayed much lower activity and affinity toward ethanol than other alcohols including butanol, hexanol, cyclohexylmethanol, and benzyl alcohol. 32,33) Moreover, SULT2A1 showed higher catalytic efficiency toward primary aliphatic alcohols with increasing carbon chain length. 33) It is therefore possible that the short carbon chain length of ethanol may be the reason for its not being a preferable substrate for SULT2A1.…”

Steroid Sulfotransferases

“…Biochemistry. HSTs isolated from rat and human liver tissue, commonly referred to as dehydroepiandrosterone sulfotransferase (DST), appear to have broad substrate specificities; that is, while they prefer dehydroepiandrosterone (3/3-hydroxy acceptor site) as substrate, they also act on such steroids as androsterone (3a-hydroxy acceptor site), testosterone (17j3-hydroxy acceptor site), and estrone or 17j3-estradiol (phenolic acceptor site and /or 17/3-hydroxy acceptor site) as well as certain nonsteroidal alcohols (131)(132)(133)(134). A rat liver HST purified by Marcus et al (132) has a molecular mass of 32 kDa and exhibits the highest efficiency (V max /K m ) for dehydroepiandrosterone, and while the K m for testosterone and 17j3-estradiol is lower than that for dehydroepiandrosterone, it sulfonates testosterone, 17j8-estradiol, and androsterone with relatively low efficiency; furthermore, little activity is demonstrated toward cortisol and corticosterone.…”

The fusion of genomes leads to more options: A comparative investigation on the desulfo-glucosinolate sulfotransferases of Brassica napus and homologous proteins of Arabidopsis thaliana

“…Members of the sulfotransferase (SOT) (EC 2.8.2.-) protein family catalyze the transfer of a sulfate group from the co-substrate 3 0 -phosphoadenosine 5 0 -phosphosulfate (PAPS) to a hydroxyl group of different kinds of substrates (Lyon and Jakoby, 1980). In almost all investigated organisms SOTs are found.…”