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ENZYME entry: EC 2.4.99.12
| Accepted Name |
|---|
| lipid IVA 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. |
| lipid IVA KDO transferase. |
| Reaction catalysed |
|---|
| CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) <=> alpha-Kdo-(2->6)-lipid IVA + CMP + H(+) |
| Comment(s) |
|---|
- The enzyme from Escherichia coli is bifunctional and transfers two
3-deoxy-D-manno-oct-2-ulosonate residues to lipid IVA (cf.
EC 2.4.99.13).
- The monofunctional enzymes from Bordetella pertusis, Aquifex aeolicus
and Haemophilus influenzae catalyze the transfer of a single 3-D-
manno-oct-2-ulosonate residue from CMP-3-D-manno-oct-2-ulosonate to
lipid IVA.
- The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-
oct-2-ulosonate residues and generate genus-specific epitopes.
|
| Cross-references |
|---|
| BRENDA | 2.4.99.12 |
| EC2PDB | 2.4.99.12 |
| ExplorEnz | 2.4.99.12 |
| PRIAM enzyme-specific profiles | 2.4.99.12 |
| KEGG Ligand Database for Enzyme Nomenclature | 2.4.99.12 |
| IUBMB Enzyme Nomenclature | 2.4.99.12 |
| IntEnz | 2.4.99.12 |
| MEDLINE | Find literature relating to 2.4.99.12 |
| MetaCyc | 2.4.99.12 |
| Rhea expert-curated reactions | 2.4.99.12 |
| UniProtKB/Swiss-Prot |
| O66663, KDTA_AQUAE; | Q8VZA5, KDTA_ARATH; | Q45374, KDTA_BORPT; |
| Q9PKI5, KDTA_CHLMU; | F0T4D1, KDTA_CHLP6; | Q46222, KDTA_CHLPN; |
| B0B9V8, KDTA_CHLT2; | Q3KMF4, KDTA_CHLTA; | P0CE14, KDTA_CHLTR; |
| P0AC77, KDTA_ECO57; | P0AC76, KDTA_ECOL6; | P0AC75, KDTA_ECOLI; |
| P44806, KDTA_HAEIN; | Q1RGU8, KDTA_RICBR; | Q92JE9, KDTA_RICCN; |
| Q4UND5, KDTA_RICFE; | Q9ZE58, KDTA_RICPR; | Q68XV7, KDTA_RICTY; |
|
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 2.4.99.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.4.-.-
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