3-deoxy-8-phosphooctulonate synthase
| 3-deoxy-8-phosphooctulonate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.5.1.55 | ||||||||
| CAS number | 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 | ||||||||
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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 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. This enzyme participates in lipopolysaccharide biosynthesis.
Structural studies
As of late 2007, 22 structures have been solved for this class of enzymes, with PDB accession codes 1O60, 1PHQ, 1PHW, 1PL9, 1Q3N, 1T8X, 1T96, 1T99, 1X6U, 1X8F, 1ZHA, 1ZJI, 2A21, 2A2I, 2EF9, 2NWR, 2NWS, 2NX1, 2NX3, 2NXG, 2NXH, and 2NXI.
References
- LEVIN DH; RACKER E (1959). "Condensation of arabinose 5-phosphate and phosphorylenol pyruvate by 2-keto-3-deoxy-8-phosphooctonic acid synthetase". J. Biol. Chem. 234: 2532&ndash, 9. PMID 14416200.
- Krosky DJ; Alm R; Berg M; Carmel G; Tummino PJ; Xu B; Yang W (2002). "Helicobacter pylori 3-deoxy-D-manno-octulosonate-8-phosphate (KDO-8-P) synthase is a zinc-metalloenzyme". Biochim. Biophys. Acta. 1594 (2): 297&ndash, 306. doi:10.1016/S0167-4838(01)00319-3. PMID 11904225.
- Asojo O; Friedman J; Adir N; Belakhov V; Shoham Y; Baasov T (2001). "Crystal structures of KDOP synthase in its binary complexes with the substrate phosphoenolpyruvate and with a mechanism-based inhibitor". Biochemistry. 40 (21): 6326&ndash, 34. doi:10.1021/bi010339d. PMID 11371194.