3-deoxy-8-phosphooctulonate synthase

From Wikipedia, the free encyclopedia

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 $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 2.5.1.55
BRENDA references for 2.5.1.55 (Recommended.)
PubMed references for 2.5.1.55
PubMed Central references for 2.5.1.55
Google Scholar references for 2.5.1.55
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: 2532–9. 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: 297–306. 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: 6326–34. doi:10.1021/bi010339d. PMID 11371194.