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Your query returned 1 entry. Printable version
EC | 2.8.2.30 | ||||||||
Accepted name: | [heparan sulfate]-glucosamine 3-sulfotransferase 3 | ||||||||
Reaction: | 3′-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3′,5′-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate | ||||||||
Glossary: | 3′-phosphoadenylyl sulfate = PAPS heparan sulfate: for definition click here |
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Other name(s): | 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase | ||||||||
Systematic name: | 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfonotransferase | ||||||||
Comments: | Two major substrates contain the tetrasaccharides: → undetermined 2-sulfo-uronic acid→ GlcN2S→ IdoA2S→ GlcN*→ and → undetermined 2-sulfo-uronic acid→ GlcN2S→ IdoA2S→ GlcN6S*→ (symbols as in 2-Carb-38) with modification of the N-unsubstituted glucosamine residue (shown with an asterisk) [1,4]. 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 [2]. There are two isozymes, known as 3-OST-3A and 3-OST-3B, which have identical catalytic domains but are encoded by different mammalian genes [3]. 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 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)]. | ||||||||
Links to other databases: | BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB | ||||||||
References: |
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