EC 2.8.2.23 - [heparan sulfate]-glucosamine 3-sulfotransferase 1

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IntEnz Enzyme Nomenclature
EC 2.8.2.23

Names

Accepted name:
[heparan sulfate]-glucosamine 3-sulfotransferase 1
Other names:
3'-phosphoadenylyl-sulfate:heparin-glucosamine 3-O-sulfotransferase
glucosaminyl 3-O-sulfotransferase
heparan sulfate D-glucosaminyl 3-O-sulfotransferase
heparin-glucosamine 3-O-sulfotransferase
isoform/isozyme 1 (3-OST-1, HS3ST1)
Systematic name:
3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008467
CAS Registry Number: 118113-79-4
UniProtKB/Swiss-Prot:

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: 15474-15484 (1988). [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: 27063-27071 (1996). [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: 27072-27082 (1996). [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: 28008-28019 (1997). [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: 5681-5691 (1999). [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: 28806-28813 (2001). [PMID: 11375390]

[EC 2.8.2.23 created 1992, modified 2001]