| Scymnol sulfotransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.8.2.32 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a scymnol sulfotransferase (EC 2.8.2.32) is an enzyme that catalyzes the chemical reaction
- 3'-Phosphoadenosine-5'-phosphosulfate + 5beta-scymnol adenosine 3',5'-bisphosphate + 5beta-scymnol sulfate
Thus, the two substrates of this enzyme are 3'-Phosphoadenosine-5'-phosphosulfate and 5beta-scymnol, whereas its two products are adenosine 3',5'-bisphosphate and 5beta-scymnol sulfate.
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'-Phosphoadenosine-5'-phosphosulfate:5beta-scymnol sulfotransferase.
References
- Macrides TA, Faktor DA, Kalafatis N, Amiet RG (1994). "Enzymic sulfation of bile salts. Partial purification and characterization of an enzyme from the liver of the shark Heterodontus portusjacksoni that catalyses the sulfation of the shark bile steroid 5 beta-scymnol". Comp. Biochem. Physiol. B. 107 (3): 461–9. doi:10.1016/0305-0491(94)90212-7. PMID 7749614.
- Pettigrew NE, Wright PF, Macrides TA (1998). "Investigation of 5beta-scymnol sulfotransferase from the kidney and testes of Heterodontus portusjacksoni". Comp. Biochem. Physiol. 121: 243–249.
- Pettigrew NE, Wright PF, Macrides TA (1998). "5beta-Scymnol sulfotransferase isolated from the tissues of an Australian shark species". Comp. Biochem. Physiol. 121: 299–307.
- Pettigrew NE, Wright PF, Macrides TA (1998). "5beta-scymnol sulfotransferase isolated from the liver of two Australian ray species". Comp. Biochem. Physiol. 121: 341–348.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.