3-deoxy-8-phosphooctulonate synthase
| 3-deoxy-8-phosphooctulonate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.55 | ||||||||
| CAS no. | 9026-96-4 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
3-deoxy-8-phosphooctulonate synthase (EC 2.5.1.55) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme first characterised from Pseudomonas aeruginosa are phosphoenolpyruvate, D-arabinose 5-phosphate, and water. Its products are 3-deoxy-α-D-manno-2-octulosonic acid 8-phosphate (3-deoxy-8-phosphooctulonic acid) and orthophosphate (Pi).[1] The enzyme isolated from Helicobacter pylori was shown to be a zinc-containing metalloprotein.[2] Its crystal structure has been determined.[3]
Nomenclature
This enzyme is a transferase, 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. It is part of the pathway to nucleotide sugars.[4]
References
- ↑ 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 (10): 2532–9. doi:10.1016/S0021-9258(18)69733-9. 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.
- ↑ Enzyme 2.5.1.55 at KEGG Pathway Database.