Structural and biochemical characterization of human mitochondrial branched-chain α-ketoacid dehydrogenase phosphatase.

@article{Wynn2012StructuralAB,
  title={Structural and biochemical characterization of human mitochondrial branched-chain α-ketoacid dehydrogenase phosphatase.},
  author={Richard Max Wynn and Jun Li and Chad A. Brautigam and Jacinta L. Chuang and David T Chuang},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 12},
  pages={
          9178-92
        }
}
The branched-chain α-ketoacid dehydrogenase phosphatase (BDP) component of the human branched-chain α-ketoacid dehydrogenase complex (BCKDC) has been expressed in Escherichia coli and purified in the soluble form. The monomeric BDP shows a strict dependence on Mn(2+) ions for phosphatase activity, whereas Mg(2+) and Ca(2+) ions do not support catalysis. Metal binding constants for BDP, determined by competition isothermal titration calorimetry, are 2.4 nm and 10 μm for Mn(2+) and Mg(2+) ions… CONTINUE READING
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