1.1.1.267	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+	active site structure	-, 671075	
1.1.1.267	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+	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	675038	
1.1.1.267	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+	mechanism	286427	
1.1.1.267	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+	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	724374	
1.1.1.267	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+	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	724346	
1.1.1.267	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+	reaction mechanism	675577	
1.1.1.267	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+	reaction mechanism via 2-C-methylerythrose 4-phosphate intermediate	672538	
1.1.1.267	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+	retro-aldol/aldol mechanism	684434	
1.1.1.267	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+	steady-state random mechanism	654748	
1.1.1.267	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+	stereochemistry	286421	
1.1.1.267	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+	the conserved active site residue Trp204 is important in catalysis	671590	
1.1.1.267	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+	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	672040