steady-state kinetic mechanism, where phosphoenolpyruvate binding precedes that of D-arabinose-5-phosphate, followed by the ordered release of phosphate and 3-deoxy-D-manno-2-octulosonate 8-phosphate
bisphosphate intermediate formed during the initial step of synthesis may have the pyranose structure with the anomeric phosphate located in the beta-configuration
quantum mechanical/molecular mechanical simulations of both the enzymatic and non-enzymatic synthesis of 2-dehydro-3-deoxy-D-octonate 8-phosphate reveal the mechanism underlying the switch between metal and non-metal dependent catalysis. The conversion is possible because the metal is not involved in an activation process, but primarily contributes to orienting properly the reactants to lower the activation energy, an action easily mimicked by amino acid side-chains
the catalytic mechanism is thought to occur by correct substrate proximity and orientation through a series of sequential conformational changes in which phosphoenolpyruvate binding precedes that of D-arabinose 5-phosphate and the release of inorganic phosphate (Pi) precedes dissociation of the 3-deoxy-D-manno-octulosonate 8-phosphate product