ENZYME entry: EC 2.8.2.23

Accepted Name
[Heparan sulfate]-glucosamine 3-sulfotransferase 1.
Alternative Name(s)
3'-phosphoadenylyl-sulfate:heparin-glucosamine 3-O-sulfotransferase.
3-OST-1.
Glucosaminyl 3-O-sulfotransferase.
Heparan sulfate D-glucosaminyl 3-O-sulfotransferase.
Heparin-glucosamine 3-O-sulfotransferase.
Reaction catalysed
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine <=> adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
Comment(s)
  • This enzyme differs from EC 2.8.2.29 and EC 2.8.2.30 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->.
  • 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->.
  • 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.
Cross-references
BRENDA2.8.2.23
EC2PDB2.8.2.23
ExplorEnz2.8.2.23
PRIAM enzyme-specific profiles2.8.2.23
KEGG Ligand Database for Enzyme Nomenclature2.8.2.23
IUBMB Enzyme Nomenclature2.8.2.23
IntEnz2.8.2.23
MEDLINEFind literature relating to 2.8.2.23
MetaCyc2.8.2.23
UniProtKB/Swiss-Prot
O14792, HS3S1_HUMAN;  O35310, HS3S1_MOUSE;  Q9ESG5, HS3S1_RAT;  
Q9Y661, HS3S4_HUMAN;  Q8IZT8, HS3S5_HUMAN;  Q8BSL4, HS3S5_MOUSE;  
Q96QI5, HS3S6_HUMAN;  Q5GFD5, HS3S6_MOUSE;  Q8BKN6, HS3SA_MOUSE;  

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.8.2.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.8.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-