ENZYME entry: EC 2.8.2.30
| Accepted Name |
| [Heparan sulfate]-glucosamine 3-sulfotransferase 3.
|
| Alternative Name(s) |
| 3-OST-3. |
| 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 |
| Comment(s) |
- 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 2.8.2.23) and it does not modify glucosamine
preceded by GlcA2S (unlike EC 2.8.2.29).
|
| Cross-references |
| BRENDA | 2.8.2.30 |
| EC2PDB | 2.8.2.30 |
| ExplorEnz | 2.8.2.30 |
| PRIAM enzyme-specific profiles | 2.8.2.30 |
| KEGG Ligand Database for Enzyme Nomenclature | 2.8.2.30 |
| IUBMB Enzyme Nomenclature | 2.8.2.30 |
| IntEnz | 2.8.2.30 |
| MEDLINE | Find literature relating to 2.8.2.30 |
| MetaCyc | 2.8.2.30 |
| UniProtKB/Swiss-Prot |
|
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