Thiol sulfotransferase

In enzymology, a thiol sulfotransferase (EC 2.8.2.16) is an enzyme that catalyzes the chemical reaction

3'-phosphoadenylyl sulfate + a thiol 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 (1976). "The adenosine-5'-phosphosulfate sulfotransferase from spinach (Spinacea oleracea L.). Stabilization, partial purification, and properties". Planta. 130 (3): 257–263. doi:10.1007/BF00387830. 
• 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.