Perturbing the hydrophobic pocket of mandelate racemase to probe phenyl motion during catalysis.

@article{Siddiqi2005PerturbingTH,
  title={Perturbing the hydrophobic pocket of mandelate racemase to probe phenyl motion during catalysis.},
  author={Ferhan S. Siddiqi and Jennifer R Bourque and HaiYan Jiang and Marieke Gardner and Martin St. Maurice and Christian Blouin and Stephen L. Bearne},
  journal={Biochemistry},
  year={2005},
  volume={44 25},
  pages={9013-21}
}
Mandelate racemase (MR, EC 5.1.2.2) from Pseudomonas putida catalyzes the Mg(2+)-dependent 1,1-proton transfer that interconverts the enantiomers of mandelate. Crystal structures of MR reveal that the phenyl group of all ground-state ligands is located within a hydrophobic cavity, remote from the site of proton abstraction. MR forms numerous electrostatic and H-bonding interactions with the alpha-OH and carboxyl groups of the substrate, suggesting that these polar groups may remain relatively… CONTINUE READING