Active site hydrophobic residues impact hydrogen tunneling differently in a thermophilic alcohol dehydrogenase at optimal versus nonoptimal temperatures.

@article{Nagel2012ActiveSH,
  title={Active site hydrophobic residues impact hydrogen tunneling differently in a thermophilic alcohol dehydrogenase at optimal versus nonoptimal temperatures.},
  author={Zachary D. Nagel and Corey Wayne Meadows and Ming Ling Dong and Brian J. Bahnson and Judith P Klinman},
  journal={Biochemistry},
  year={2012},
  volume={51 20},
  pages={
          4147-56
        }
}
A growing body of data suggests that protein motion plays an important role in enzyme catalysis. Two highly conserved hydrophobic active site residues in the cofactor-binding pocket of ht-ADH (Leu176 and V260) have been mutated to a series of hydrophobic side chains of smaller size, as well as one deletion mutant, L176Δ. Mutations decrease k(cat) and increase K(M)(NAD(+)). Most of the observed decreases in effects on k(cat) at pH 7.0 are due to an upward shift in the optimal pH for catalysis; a… CONTINUE READING
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