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.

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• 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.
• 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.