Reaction: phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
Other name(s): 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; phospho-2-keto-3-deoxyoctonate aldolase
Systematic name: phosphoenolpyruvate:D-arabinose-5-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-96-4
1. Levin, D.H. and Racker, E. Condensation of arabinose 5-phosphate and phosphorylenol pyruvate by 2-keto-3-deoxy-8-phosphooctonic acid synthetase. J. Biol. Chem. 234 (1959) 2532-25339.
2. Krosky, D.J., Alm, R., Berg, M., Carmel, G., Tummino, P.J., Xu, B. and Yang, W. Helicobacter pylori 3-deoxy-D-manno-octulosonate-8-phosphate (KDO-8-P) synthase is a zinc-metalloenzyme. Biochim. Biophys. Acta 1594 (2002) 297-306. [PMID: 11904225]
3. Asojo, O., Friedman, J., Adir, N., Belakhov, V., Shoham, Y. and Baasov, T. Crystal structures of KDOP synthase in its binary complexes with the substrate phosphoenolpyruvate and with a mechanism-based inhibitor. Biochemistry 40 (2001) 6326-6334. [PMID: 11371194]