(heparan sulfate)-glucosamine 3-sulfotransferase 3
- 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine Failed to parse (MathML with SVG or PNG fallback (recommended for modern browsers and accessibility tools): Invalid response ("Math extension cannot connect to Restbase.") from server "https://api.formulasearchengine.com/v1/":): \rightleftharpoons 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.
- IUBMB entry for 220.127.116.11
- BRENDA references for 18.104.22.168 (Recommended.)
- PubMed references for 22.214.171.124
- PubMed Central references for 126.96.36.199
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- RD (1999). "Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A sulfates N-unsubstituted glucosamine residues". J. Biol. Chem. 274: 38155–62. 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: 13–22. 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: 5170–84. PMID 9988767.
- Rosenberg RD (1999). "Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities". J. Biol. Chem. 274: 5185–92. PMID 9988768.