(heparan sulfate)-glucosamine 3-sulfotransferase 3

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(heparan sulfate)-glucosamine 3-sulfotransferase 3
Identifiers
EC number 2.8.2.30
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 3 (EC 2.8.2.30) 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. This enzyme participates in heparan sulfate biosynthesis and glycan structures - biosynthesis 1.

References[edit]

  • RD; Shriver, Z; Blaiklock, P; Yoshida, K; Sasisekharan, R; Rosenberg, RD (1999). "Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A sulfates N-unsubstituted glucosamine residues". J. Biol. Chem. 274 (53): 38155–62. doi:10.1074/jbc.274.53.38155. PMID 10608887. 
  • Eisenberg RJ, Rosenberg RD, Spear PG (1999). "A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry". Cell. 99 (1): 13–22. doi:10.1016/S0092-8674(00)80058-6. PMID 10520990. 
  • Jenkins NA, Rosenberg RD (1999). "Multiple isoforms of heparan 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 isoforms reveals novel substrate specificities". J. Biol. Chem. 274 (8): 5185–92. doi:10.1074/jbc.274.8.5185. PMID 9988768.