In enzymology, a thiol sulfotransferase (EC 2.8.2.16) is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + a thiol ⇌ {\displaystyle \rightleftharpoons } adenosine 3',5'-bisphosphate + an S-alkyl thiosulfate Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and thiol, whereas its two products are adenosine 3',5'-bisphosphate and S-alkyl thiosulfate. This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:thiol S-sulfotransferase. Other names in common use include phosphoadenylylsulfate-thiol sulfotransferase, PAPS sulfotransferase, and adenosine 3'-phosphate 5'-sulphatophosphate sulfotransferase.
References
Schmidt A (January 1976). "The adenosine-5'-phosphosulfate sulfotransferase from spinach (Spinacea oleracea L.). Stabilization, partial purification, and properties". Planta. 130 (3): 257–63. Bibcode:1976Plant.130..257S. doi:10.1007/BF00387830. PMID 24424637. Schmidt A, Christen U (1979). "A PAPS-dependent sulfotransferase in Cyanophora paradoxa inhibited by 5'-AMP, 5'-ADP and APS". Z. Naturforsch. C: Biosci. 34: 222–228. doi:10.1515/znc-1979-3-411. Tsang M (1976). "L.-S. and Schiff, J.A. Studies of sulfate utilization by algae. 17 Reactions of the adenosine 5'-phosphosulfate (APS) sulfotransferase from Chlorella and studies of model reactions which explain the diversity of side products with thiols". Plant Cell Physiol. 17: 1209–1220.
