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 (E. coli) + 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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