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.
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References
Further reading
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. PMID14416200.
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. PMID11904225.
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. PMID11371194.
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