Thioredoxin-mediated reductive activation of a protein kinase for the regulatory phosphorylation of C4-form phosphoenolpyruvate carboxylase from maize.

@article{Saze2001ThioredoxinmediatedRA,
  title={Thioredoxin-mediated reductive activation of a protein kinase for the regulatory phosphorylation of C4-form phosphoenolpyruvate carboxylase from maize.},
  author={H Saze and Yoshihisa Ueno and Toru Hisabori and Hidenori Hayashi and K. Izui},
  journal={Plant & cell physiology},
  year={2001},
  volume={42 12},
  pages={1295-302}
}
The activity of phosphoenolpyruvate carboxylase (PEPC, EC4.1.1.31) for the C4 photosynthesis is known to be regulated mainly in response to light/dark transitions through reversible phosphorylation by a specific protein kinase (PK). PEPC-PK with an M(r) of 30 kDa was purified about 1.4 million-fold to homogeneity from maize leaves and characterized. The purified PEPC-PK was readily inactivated under mild oxidative conditions, but the activity could be recovered by dithiothreitol (DTT). The… CONTINUE READING

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