Multiple substrate binding states and chiral recognition in cofactor-independent glutamate racemase: a molecular dynamics study.

@article{Mbitz2004MultipleSB,
  title={Multiple substrate binding states and chiral recognition in cofactor-independent glutamate racemase: a molecular dynamics study.},
  author={Henrik M{\"o}bitz and Thomas C. Bruice},
  journal={Biochemistry},
  year={2004},
  volume={43 30},
  pages={9685-94}
}
Glutamate racemase (MurI) catalyzes the racemization of glutamate; two cysteine residues serve as catalytic acid and base. On the basis of the crystal structure of MurI from the hyperthermophilic bacterium Aquifex pyrophilus, we performed molecular dynamics (MD) simulations of six different systems to investigate stereochemistry, substrate ligation, and active site protonation state. The catalytic competence of individual systems was assessed by the abundance of reactive conformers. Only… CONTINUE READING

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