3-deoxy-8-phosphooctulonate synthase
| 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[edit]
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[edit]
Further reading[edit]
- 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.
