| Heparin-glucosamine 3-O-sulfotransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.8.2.23 | ||||||||
| CAS no. | 118113-79-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a [heparan sulfate]-glucosamine 3-sulfotransferase 1 (EC 2.8.2.23) is an enzyme that catalyzes the chemical reaction
- 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and heparan sulfate-glucosamine, whereas its two products are adenosine 3',5'-bisphosphate and heparan sulfate-glucosamine 3-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'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase. Other names in common use include heparin-glucosamine 3-O-sulfotransferase, 3'-phosphoadenylyl-sulfate:heparin-glucosamine 3-O-sulfotransferase, glucosaminyl 3-O-sulfotransferase, heparan sulfate D-glucosaminyl 3-O-sulfotransferase, and isoform/isozyme 1 (3-OST-1, HS3ST1). This enzyme participates in heparan sulfate biosynthesis and glycan structures - biosynthesis 1.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1VKJ and 1ZRH.
References
- Kusche M, Backstrom G, Riesenfeld J, Petitou M, Choay J, Lindahl U (1988). "Biosynthesis of heparin. O-sulfation of the antithrombin-binding region". J. Biol. Chem. 263 (30): 15474–84. PMID 3139669.
- Shworak NW, Fritze LM, Liu J, Butler LD, Rosenberg RD (1996). "Cell-free synthesis of anticoagulant heparan sulfate reveals a limiting converting activity that modifies an excess precursor pool". J. Biol. Chem. 271 (43): 27063–27071. doi:10.1074/jbc.271.43.27063. PMID 8900197.
- Liu J, Shworak NW, Fritze LM, Edelberg JM, Rosenberg RD (1996). "Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase". J. Biol. Chem. 271 (43): 27072–27082. doi:10.1074/jbc.271.43.27072. PMID 8900198.
- Rosenberg RD; Liu, J; Fritze, LM; Schwartz, JJ; Zhang, L; Logeart, D; Rosenberg, RD (1997). "Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase". J. Biol. Chem. 272 (44): 28008–28019. doi:10.1074/jbc.272.44.28008. PMID 9346953.
- Zhang L, Yoshida K, Liu J, Rosenberg RD (1999). "Anticoagulant heparan sulfate precursor structures in F9 embryonal carcinoma cells". J. Biol. Chem. 274 (9): 5681–5691. doi:10.1074/jbc.274.9.5681. PMID 10026187.
- RD; Lawrence, R; Schwartz, JJ; Bai, X; Wei, G; Esko, JD; Rosenberg, RD (2001). "The effect of precursor structures on the action of glucosaminyl 3-O-sulfotransferase-1 and the biosynthesis of anticoagulant heparan sulfate". J. Biol. Chem. 276 (31): 28806–28813. doi:10.1074/jbc.M100204200. PMID 11375390.