Biology:3-deoxy-8-phosphooctulonate synthase

From HandWiki
Short description: Enzyme
3-deoxy-8-phosphooctulonate synthase
Identifiers
EC number2.5.1.55
CAS number9026-96-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / 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 [math]\displaystyle{ \rightleftharpoons }[/math] 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

  • "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. October 1959. PMID 14416200. 
  • "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. February 2002. doi:10.1016/S0167-4838(01)00319-3. PMID 11904225. 
  • "Crystal structures of KDOP synthase in its binary complexes with the substrate phosphoenolpyruvate and with a mechanism-based inhibitor". Biochemistry 40 (21): 6326–34. May 2001. doi:10.1021/bi010339d. PMID 11371194.