highly conserved active site structure, active site residues Asp157, Glu159, and Glu241, residue His219 is essential for placing the substrate in the active site for optimal catalysis
the reaction does not exhibit burst kinetics for either substrate, indicating that product release is not rate-limiting, the rearrangement step, which precedes hydride transfer, is rate-limiting for 1-deoxy-D-xylulose 5-phosphate but becomes partially ratelimiting for 1-fluoro-1-deoxy-D-xylulose 5-phosphate, thus, rearrangement appears to be enhanced by substitution of a hydrogen atom in the methyl group of 1-deoxy-D-xylulose 5-phosphate by fluorine, consistent with a retro-aldol/aldol mechanism for the rearrangement during conversion of 1-deoxy-D-xylulose 5-phosphate to 2-C-methyl-D-erythritol 4-phosphate
random ordered mechanism, though binding of NADPH first is preferential at 0.2 mM due to its low Km. Conformational equilibrium between a predominant, inactive open form and a minor, active closed form of the unliganded enzyme, overview
random substrate binding and ordered release of NADP+ followed by partially rate-limiting release of 2-C-methyl-D-erythritol 4-phosphate, transient generation of MtDXR-NADPH-MEP ternary complex, kinetic analysis and modeling, overview