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Regulation of Pyruvate Dehydrogenase by End Product Inhibition and by Phosphorylation

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Metabolic Interconversion of Enzymes 1975

Part of the book series: Proceedings in Life Sciences ((LIFE SCIENCES))

Abstract

Pyruvate dehydrogenase is regulated by end product inhibition by acetyl CoA (competitive with CoA) , NADH 2 (competitive NAD) and acetoin (competitive pyruvate); and through inactivation by phosphorylation catalysed by an intrinsic kinase utilising ATPMg++ and reactivation by a phosphatase. Recent studies in this laboratory have been concerned with the site of action of phosphorylation on the overall reaction sequence of pyruvate dehydrogenase; the relationship between end-product inhibition and phosphorylation and the mechanism whereby oxidation of fatty acids and ketone bodies leads to phosphorylation and inactivation of pyruvate dehydrogenase; with the action of insulin on pyruvate dehydrogenase, and the role of calcium; and with the biochemical pharmacology of dichloroacetate.

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© 1976 Springer-Verlag Berlin Heidelberg

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Randle, P.J., Denton, R.M. (1976). Regulation of Pyruvate Dehydrogenase by End Product Inhibition and by Phosphorylation. In: Shaltiel, S. (eds) Metabolic Interconversion of Enzymes 1975. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-66461-8_17

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  • DOI: https://doi.org/10.1007/978-3-642-66461-8_17

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-66463-2

  • Online ISBN: 978-3-642-66461-8

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