Biochemical characterization of prephenate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicus.

@article{Bonvin2006BiochemicalCO,
  title={Biochemical characterization of prephenate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicus.},
  author={Julie Bonvin and Raphael A Aponte and Maria Marcantonio and Sasha Anna Singh and Dinesh Christendat and Joanne L. Turnbull},
  journal={Protein science : a publication of the Protein Society},
  year={2006},
  volume={15 6},
  pages={1417-32}
}
A monofunctional prephenate dehydrogenase (PD) from Aquifex aeolicus was expressed as a His-tagged protein in Escherichia coli and was purified by nickel affinity chromatography allowing the first biochemical and biophysical characterization of a thermostable PD. A. aeolicus PD is susceptible to proteolysis. In this report, the properties of the full-length PD are compared with one of these products, an N-terminally truncated protein variant (Delta19PD) also expressed recombinantly in E. coli… CONTINUE READING

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