ExplorEnz: EC 2.8.2.23

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2.8.2.23

Accepted name:

[heparan sulfate]-glucosamine 3-sulfotransferase 1

Reaction:

3′-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3′,5′-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate

Glossary:

3′-phosphoadenylyl sulfate = PAPS

Other name(s):

heparin-glucosamine 3-O-sulfotransferase; 3′-phosphoadenylyl-sulfate:heparin-glucosamine 3-O-sulfotransferase; glucosaminyl 3-O-sulfotransferase; heparan sulfate D-glucosaminyl 3-O-sulfotransferase; isoform/isozyme 1 (3-OST-1, HS3ST1); 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase

Systematic name:

3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfonotransferase

Comments:

This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases [EC 2.8.2.29 ([heparan sulfate]-glucosamine 3-sulfotransferase 2) and EC 2.8.2.30 ([heparan sulfate]-glucosamine 3-sulfotransferase 3)] by being the most selective for a precursor of the antithrombin-binding site. It has a minimal acceptor sequence of: → GlcNAc₆S→ GlcA→ GlcN₂S*+/-6S→ IdoA2S→ GlcN₂S→ , the asterisk marking the target (symbols as in 2-Carb-38) using +/- to mean the presence or absence of a substituent, and > to separate a predominant structure from a minor one. Thus Glc(N₂S > NAc) means a residue of glucosamine where the N carries a sulfo group mainly but occasionally an acetyl group. [1-4]. It can also modify other precursor sequences within heparan sulfate but this action does not create functional antithrombin-binding sites. These precursors are variants of the consensus sequence: → Glc(N₂S > NAc)+/-6S→ GlcA→ GlcN₂S*+/-6S→ GlcA > IdoA⁺/-2S→ Glc(N₂S/NAc)+/-6S→ [5]. If the heparan sulfate substrate lacks 2-O-sulfation of GlcA residues, then enzyme specificity is expanded to modify selected glucosamine residues preceded by IdoA as well as GlcA [6].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 183257-54-7

References:

1.	Kusche, M., Backström, G., Riesenfeld, J., Pepitou, M., Choay, J. and Lindahl, U. Biosynthesis of heparin. O-Sulfation of the antithrombin-binding region. J. Biol. Chem. 263 (1988) 15474–15484. [PMID: 3139669]
2.	Shworak, N.W., Fritze, L.M.S., Liu, J., Butler, L.D. and Rosenberg, R.D. Cell-free synthesis of anticoagulant heparan sulfate reveals a limiting activity which modifies a nonlimiting precursor pool. J. Biol. Chem. 271 (1996) 27063–27071. [DOI] [PMID: 8900197]
3.	Liu, J., Shworak, N.W., Fritze, L.M.S., Edelberg, J.M. and Rosenberg, R.D. Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. J. Biol. Chem. 271 (1996) 27072–27082. [DOI] [PMID: 8900198]
4.	Shworak, N.W., Liu, J., Fritze, L.M.S., Schwartz, J.J., Zhang, L., Logeart, D. and Rosenberg, R.D. Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase. J. Biol. Chem. 272 (1997) 28008–28019. [DOI] [PMID: 9346953]
5.	Zhang, L., Yoshida, K., Liu, J. and Rosenberg, R.D. Anticoagulant heparan sulfate precursor structures in F9 embryonal carcinoma cells. J. Biol. Chem. 274 (1999) 5681–5691. [DOI] [PMID: 10026187]
6.	Zhang, L., Lawrence, R., Schwartz, J.J., Bai, X. , Wei., G, Esko, J.D. and Rosenberg, R.D. 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 (2001) 28806–28813. [DOI] [PMID: 11375390]

[EC 2.8.2.23 created 1992, modified 2001]