Contributions of valine-292 in the nicotinamide binding site of liver alcohol dehydrogenase and dynamics to catalysis.

@article{Rubach2001ContributionsOV,
  title={Contributions of valine-292 in the nicotinamide binding site of liver alcohol dehydrogenase and dynamics to catalysis.},
  author={Jon K. Rubach and Subramanyan Ramaswamy and Bryce V Plapp},
  journal={Biochemistry},
  year={2001},
  volume={40 42},
  pages={12686-94}
}
The participation of Val-292 in catalysis by alcohol dehydrogenase and the involvement of dynamics were investigated. Val-292 interacts with the nicotinamide ring of the bound coenzyme and may facilitate hydride transfer. The substitution of Val-292 with Ser (V292S) increases the dissociation constants for the coenzymes (NAD(+) by 50-fold, NADH by 75-fold… CONTINUE READING