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Results 1 - 10 of 12 > >>
EC Number
Reaction
Commentary
Reference
2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
active site structure
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
2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
mechanism
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
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
2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
reaction mechanism
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
2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
retro-aldol/aldol mechanism
2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
steady-state random mechanism
2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
stereochemistry
Results 1 - 10 of 12 > >>