Regulation of glutamate dehydrogenase by reversible ADP-ribosylation in mitochondria.

@article{HerreroYraola2001RegulationOG,
  title={Regulation of glutamate dehydrogenase by reversible ADP-ribosylation in mitochondria.},
  author={A Herrero-Yraola and S M Bakhit and Peter Franke and Christoph Weise and Manfred Schweiger and Dierk Jorcke and Mathias Ziegler},
  journal={The EMBO journal},
  year={2001},
  volume={20 10},
  pages={2404-12}
}
Mitochondrial ADP-ribosylation leads to modification of two proteins of approximately 26 and 53 kDA: The nature of these proteins and, hence, the physiological consequences of their modification have remained unknown. Here, a 55 kDa protein, glutamate dehydrogenase (GDH), was established as a specific acceptor for enzymatic, cysteine-specific ADP-ribosylation in mitochondria. The modified protein was isolated from the mitochondrial preparation and identified as GDH by N-terminal sequencing and… CONTINUE READING