| 3-deoxy-8-phosphooctulonate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.55 | ||||||||
| CAS no. | 9026-96-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a 3-deoxy-8-phosphooctulonate synthase (EC 2.5.1.55) is an enzyme that catalyzes the chemical reaction
- phosphoenolpyruvate + D-arabinose 5-phosphate + H2O 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
The 3 substrates of this enzyme are phosphoenolpyruvate, D-arabinose 5-phosphate, and H2O, whereas its two products are 2-dehydro-3-deoxy-D-octonate 8-phosphate and phosphate.
This enzyme participates in lipopolysaccharide biosynthesis.
Nomenclature
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is phosphoenolpyruvate:D-arabinose-5-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming). Other names in common use include 2-dehydro-3-deoxy-D-octonate-8-phosphate, D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating), 2-dehydro-3-deoxy-phosphooctonate aldolase, 2-keto-3-deoxy-8-phosphooctonic synthetase, 3-deoxy-D-manno-octulosonate-8-phosphate synthase, 3-deoxy-D-mannooctulosonate-8-phosphate synthetase, 3-deoxyoctulosonic 8-phosphate synthetase, KDOP synthase, and phospho-2-keto-3-deoxyoctonate aldolase.
References
Further reading
- Levin DH, Racker E (October 1959). "Condensation of arabinose 5-phosphate and phosphorylenol pyruvate by 2-keto-3-deoxy-8-phosphooctonic acid synthetase". The Journal of Biological Chemistry. 234: 2532–9. PMID 14416200.
- Krosky DJ, Alm R, Berg M, Carmel G, Tummino PJ, Xu B, Yang W (February 2002). "Helicobacter pylori 3-deoxy-D-manno-octulosonate-8-phosphate (KDO-8-P) synthase is a zinc-metalloenzyme". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1594 (2): 297–306. doi:10.1016/S0167-4838(01)00319-3. PMID 11904225.
- Asojo O, Friedman J, Adir N, Belakhov V, Shoham Y, Baasov T (May 2001). "Crystal structures of KDOP synthase in its binary complexes with the substrate phosphoenolpyruvate and with a mechanism-based inhibitor". Biochemistry. 40 (21): 6326–34. doi:10.1021/bi010339d. PMID 11371194.