Abstract
Dichloroacetate and other halogenated carboxylic acids can activate pyruvate dehydrogenase in rat heart and in rat heart mitochondria by effecting conversion of phosphorylated (inactive) pyruvate dehydrogenase into an active (dephosphorylated) form. These compounds are inhibitors of pig heart pyruvate dehydrogenase kinase. Pig heart pyruvate dehydrogenase phosphate phosphatase requires both Mg2+and Ca2+ for activity. Evidence is given for a dual metal requirement of the phosphatase in rat fat cell mitochondria. It is concluded that Mg2+ and Ca2+ are essential cofactors for the phosphatase but that their physiological significance as regulators remains to be established. Pig heart pyruvate dehydrogenase kinase is inhibited by high concentrations of magnesium and by low concentrations of calcium.
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Cooper, R.H., Denton, R.M., Pask, H.T., Randle, P.J., Severson, D.L., Whitehouse, S. (1974). Regulation of Mammalian Pyruvate Dehydrogenases. In: Metabolic Interconversion of Enzymes 1973. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-80817-3_11
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DOI: https://doi.org/10.1007/978-3-642-80817-3_11
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