(KDO)3-lipid IVA (2-4) 3-deoxy-D-manno-octulosonic acid transferase
(KDO)3-lipid IVA (2-4) 3-deoxy-D-manno-octulosonic acid transferase (EC 2.4.99.15, KDO transferase, waaA (gene), kdtA (gene), 3-deoxy-D-manno-oct-2-ulosonic acid transferase, 3-deoxy-manno-octulosonic acid transferase) is an enzyme with systematic name CMP-3-deoxy-D-manno-oct-2-ulosonate:(KDO)3-lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase ((2->4) glycosidic bond-forming).[1][2] This enzyme catalyses the following chemical reaction
- alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP-alpha-Kdo alpha-Kdo-(2->8)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP
| (KDO)3-lipid IVA (2-4) 3-deoxy-D-manno-octulosonic acid transferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.4.99.15 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
The enzyme from Chlamydia psittaci transfers four KDO residues to lipid A, forming a branched tetrasaccharide.
References
- Brabetz W, Lindner B, Brade H (September 2000). "Comparative analyses of secondary gene products of 3-deoxy-D-manno-oct-2-ulosonic acid transferases from Chlamydiaceae in Escherichia coli K-12". European Journal of Biochemistry. 267 (17): 5458–65. doi:10.1046/j.1432-1327.2000.01619.x. PMID 10951204.
- Holst O, Bock K, Brade L, Brade H (April 1995). "The structures of oligosaccharide bisphosphates isolated from the lipopolysaccharide of a recombinant Escherichia coli strain expressing the gene gseA [3-deoxy-D-manno-octulopyranosonic acid (Kdo) transferase] of Chlamydia psittaci 6BC". European Journal of Biochemistry. 229 (1): 194–200. doi:10.1111/j.1432-1033.1995.tb20455.x. PMID 7744029.
External links
- (KDO)3-lipid+IVA+(2-4)+3-deoxy-D-manno-octulosonic+acid+transferase at the US National Library of Medicine Medical Subject Headings (MeSH)
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