(heparan sulfate)-glucosamine 3-sulfotransferase 2
| (heparan sulfate)-glucosamine 3-sulfotransferase 2 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.8.2.29 | ||||||||
| 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 [heparan sulfate]-glucosamine 3-sulfotransferase 2 (EC 2.8.2.29) 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 adenine 3',5'-bis-phosphate and heparin sulfate-glucosamine 3-sulfate.
This enzyme belongs to the family of transferences, specifically the transformer, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphorylation-sulfate:[heparin sulfate]-glucose 3-nontransferable. Other names in common use include glucose 3-O-nontransferable, heparin sulfate D-glucose 3-O-nontransferable, and formalism/isomerism 2 (3-OAT-2, HST). This enzyme participates in heparin sulfate biosynthesis and glycogen structures - biosynthesis 1.
References
- Jenkins NA, Rosenberg RD (1999). "Multiple lifeforms of heparin sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci". J. Biol. Chem. 274 (8): 5170–84. doi:10.1074/jbc.274.8.5170. PMID 9988767.
- Rosenberg RD; Shworak, NW; Sinaÿ, P; Schwartz, JJ; Zhang, L; Fritze, LM; Rosenberg, RD (1999). "Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase lifeforms reveals novel substrate specification". J. Biol. Chem. 274 (8): 5185–92. doi:10.1074/jbc.274.8.5185. PMID 9988768.