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. 1988 Dec;88(4):1026–1030. doi: 10.1104/pp.88.4.1026

Regulation of Steady State Pyruvate Dehydrogenase Complex Activity in Plant Mitochondria 1

Reactivation Constraints

Raymond J A Budde 1, Douglas D Randall 1
PMCID: PMC1055709  PMID: 16666415

Abstract

The requirements for reactivation (dephosphorylation) of the pea (Pisum sativum L.) leaf mitochondrial pyruvate dehydrogenase complex (PDC) were studied in terms of magnesium and ATP effects with intact and permeabilized mitochondria. The requirement for high concentrations of magnesium for reactivation previously reported with partially purified PDC is shown to affect inactivation rather than reactivation. The observed rate of inactivation catalyzed by pyruvate dehydrogenase (PDH) kinase is always greater than the reactivation rate catalyzed by PDH-P phosphatase. Thus, reactivation would only occur if ATP becomes limiting. However, pyruvate which is a potent inhibitor of inactivation in the presence of thiamine pyrophosphate, results in increased PDC activity. Analysis of the dynamics of the phosphorylation-dephosphorylation cycle indicated that the covalent modification was under steady state control. The steady state activity of PDC was increased by addition of pyruvate. PDH kinase activity increased threefold during storage of mitochondria suggesting that there may be an unknown level of regulation exerted on the enzyme complex.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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