ENZYME entry: EC

Accepted Name
[Heparan sulfate]-glucosamine 3-sulfotransferase 3.
Alternative Name(s)
Glucosaminyl 3-O-sulfotransferase 3.
Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3.
Reaction catalysed
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine <=> adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
  • Two major substrates contain the tetrasaccharides: -> undetermined 2-sulfo-uronic acid->GlcN2S->IdoA2S->GlcN*-> and -> undetermined 2-sulfo-uronic acid->GlcN2S->IdoA2S->GlcN6S*-> with modification of the N-unsubstituted glucosamine residue (shown with an asterisk).
  • Modification of selected sequences containing N-sulfo-glucosamine residues cannot yet be excluded.
  • The 3-O-sulfated heparan sulfate can be utilized by Herpes simplex virus type 1 as an entry receptor to infect the target cells.
  • There are two isozymes, known as 3-OST-3(A) and 3-OST-3(B), which have identical catalytic domains but are encoded by different mammalian genes.
  • The specificity of this enzyme differs from that of the other [heparan sulfate]-glucosamine 3-sulfotransferases.
  • It is inefficient at modifying precursors of the antithrombin binding site (in contrast to EC and it does not modify glucosamine preceded by GlcA2S (unlike EC
PRIAM enzyme-specific profiles2.8.2.30
KEGG Ligand Database for Enzyme Nomenclature2.8.2.30
IUBMB Enzyme Nomenclature2.8.2.30
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