The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: [heparan sulfate]-glucosamine 3-sulfotransferase 2
Reaction: 3′-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3′,5′-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
Glossary: 3′-phosphoadenylyl sulfate = PAPS
heparan sulfate: for definition click here
Other name(s): glucosaminyl 3-O-sulfotransferase; heparan sulfate D-glucosaminyl 3-O-sulfotransferase; isoform/isozyme 2 (3-OST-2, HS3ST2); 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfonotransferase
Comments: This enzyme sulfates the residues marked with an asterisk in sequences containing at least → IdoA2S→ GlcN*→ or → GlcA2S→ GlcN*→ (symbols as in 2-Carb-38). Preference for GlcN2S vs. unmodified GlcN has not yet been established. Additional structural features are presumably required for substrate recognition, since the 3-O-sulfated residue is of low abundance, whereas the above IdoA-containing sequence is quite abundant. This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases by modifying selected glucosamine residues preceded by GlcA2S; EC ([heparan sulfate]-glucosamine 3-sulfotransferase 1) prefers GlcA or IdoA, whereas EC ([heparan sulfate]-glucosamine 3-sulfotransferase 3) prefers IdoA2S.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Shworak, N.W., Liu, J., Petros, L.M., Copeland, N.G. , Jenkins N.A. and Rosenberg, R.D. Diversity of the extensive heparan sulfate D-glucosaminyl 3-O-sulfotransferase (3-OST) multigene family. J. Biol. Chem. 274 (1999) 5170–5184. [DOI] [PMID: 9988767]
2.  Liu, J., Shworak, N.W., Sina, P., Schwartz, J.J., Zhang, L., Fritze, L.M.S. and Rosenberg, R.D. Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities. J. Biol. Chem. 274 (1999) 5185–5192. [DOI] [PMID: 9988768]
[EC created 2001]

Data © 2001–2023 IUBMB
Web site © 2005–2023 Andrew McDonald