ENZYME entry: EC 2.4.99.15
| Accepted Name |
|---|
| (Kdo)3-lipid IVA (2-4) 3-deoxy-D-manno-octulosonic acid transferase.
|
| Alternative Name(s) |
|---|
| 3-deoxy-D-manno-oct-2-ulosonic acid transferase. |
| 3-deoxy-manno-octulosonic acid transferase. |
| Kdo transferase. |
| Reaction catalysed |
|---|
| alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP-3-deoxy-beta-D-manno-octulosonate <=> alpha-Kdo-(2->8)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP + H(+) |
| Comment(s) |
|---|
| The enzyme from Chlamydia psittaci transfers four KDO residues to
lipid A, forming a branched tetrasaccharide with the structure alpha-
KDO-(2,8)-[alpha-KDO-(2,4)]-alpha-KDO-(2,4)-alpha-KDO (cf.
EC 2.4.99.12, EC 2.4.99.13 and EC 2.4.99.14).
|
| Cross-references |
|---|
| BRENDA | 2.4.99.15 |
| EC2PDB | 2.4.99.15 |
| ExplorEnz | 2.4.99.15 |
| PRIAM enzyme-specific profiles | 2.4.99.15 |
| KEGG Ligand Database for Enzyme Nomenclature | 2.4.99.15 |
| IUBMB Enzyme Nomenclature | 2.4.99.15 |
| IntEnz | 2.4.99.15 |
| MEDLINE | Find literature relating to 2.4.99.15 |
| MetaCyc | 2.4.99.15 |
| Rhea expert-curated reactions | 2.4.99.15 |
| UniProtKB/Swiss-Prot |
|
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