E. coli MEP synthase: steady-state kinetic analysis and substrate binding.

@article{Koppisch2002ECM,
  title={E. coli MEP synthase: steady-state kinetic analysis and substrate binding.},
  author={Andrew T. Koppisch and David T. Fox and Brian S. J. Blagg and C. Dale Poulter},
  journal={Biochemistry},
  year={2002},
  volume={41 1},
  pages={236-43}
}
2-C-Methyl-D-erythritol-4-phosphate synthase (MEP synthase) catalyzes the rearrangement/reduction of 1-D-deoxyxylulose-5-phosphate (DXP) to methylerythritol-4-phosphate (MEP) as the first pathway-specific reaction in the MEP biosynthetic pathway to isoprenoids. Recombinant E. coli MEP was purified by chromatography on DE-52 and phenyl-Sepharose, and its steady-state kinetic constants were determined: k(cat) = 116 +/- 8 s(-1), K(M)(DXP) = 115 +/- 25 microM, and K(M)(NADPH) = 0.5 +/- 0.2 microM… CONTINUE READING