Activation and inhibition of histone deacetylase 8 by monovalent cations.

@article{Gantt2010ActivationAI,
  title={Activation and inhibition of histone deacetylase 8 by monovalent cations.},
  author={Stephanie L Gantt and Caleb G Joseph and Carol A. Fierke},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 9},
  pages={6036-43}
}
The metal-dependent histone deacetylases (HDACs) catalyze hydrolysis of acetyl groups from acetyllysine side chains and are targets of cancer therapeutics. Two bound monovalent cations (MVCs) of unknown function have been previously observed in crystal structures of HDAC8; site 1 is near the active site, whereas site 2 is located > 20 A from the catalytic metal ion. Here we demonstrate that one bound MVC activates catalytic activity (K(1/2) = 3.4 mM for K(+)), whereas the second, weaker-binding… CONTINUE READING