Identification of a long-range protein network that modulates active site dynamics in extremophilic alcohol dehydrogenases.

@article{Nagel2013IdentificationOA,
  title={Identification of a long-range protein network that modulates active site dynamics in extremophilic alcohol dehydrogenases.},
  author={Zachary D. Nagel and Shujian Cun and Judith P Klinman},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 20},
  pages={
          14087-97
        }
}
A tetrameric thermophilic alcohol dehydrogenase from Bacillus stearothermophilus (ht-ADH) has been mutated at an aromatic side chain in the active site (Trp-87). The ht-W87A mutation results in a loss of the Arrhenius break seen at 30 °C for the wild-type enzyme and an increase in cold lability that is attributed to destabilization of the active tetrameric form. Kinetic isotope effects (KIEs) are nearly temperature-independent over the experimental temperature range, and similar in magnitude to… CONTINUE READING

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