Pressure-induced thermostabilization of glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus.

@article{Sun1999PressureinducedTO,
  title={Pressure-induced thermostabilization of glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus.},
  author={Mingshan Sun and Nicola Tolliday and C Vetriani and Frank T Robb and Douglas S Clark},
  journal={Protein science : a publication of the Protein Society},
  year={1999},
  volume={8 5},
  pages={1056-63}
}
In this paper, elevated pressures up to 750 atm (1 atm = 101 kPa) were found to have a strong stabilizing effect on two extremely thermophilic glutamate dehydrogenases (GDHs): the native enzyme from the hyperthermophile Pyrococcus furiosus (Pf), and a recombinant GDH mutant containing an extra tetrapeptide at the C-terminus (rGDHt). The presence of the tetrapeptide greatly destabilized the recombinant mutant at ambient pressure; however, the destabilizing effect was largely reversed by the… CONTINUE READING
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