   2.8.2.30 | 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. 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 isoenzymes, known as 3-OST-3A and 3-OST-3B, which have identical catalytic domains but are encoded by different mammalian genes. The specificity of this enzyme differs from that of other [heparan sulfate]-glucosamine 3-sulfotransferases. It is inefficient at modifying precursors of antithrombin binding site, in contrast to EC 2.8.2.23, [heparan sulfate]-glucosamine 3-sulfotransferase 1, and it does not modify glucosamine preceded by GlcA2S, unlike EC 2.8.2.29, [heparan sulfate]-glucosamine 3-sulfotransferase 2 |
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