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Plant Physiology 88:1031-1036 (1988)
© 1988 American Society of Plant Biologists

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Metabolism and Enzymology

Regulation of the Phosphorylation of Mitochondrial Pyruvate Dehydrogenase Complex in Situ1

Effects of Respiratory Substrates and Calcium

Raymond J. A. Budde, Tung K. Fang and Douglas D. Randall

Department of Biochemistry, University of Missouri, Columbia, Missouri 65211

The activity of the pyruvate dehydrogenase complex (PDC), as controlled by reversible phosphorylation, was studied in situ with mitochondria oxidizing dfifferent substrates. PDCs from both plant and animal tissues were inactivated when pyruvate became limiting. The PDC did not inactivate in the presence of saturating levels of pyruvate. Calcium stimulated reactivation of PDC in chicken heart but not pea (Pisum sativum L.) leaf mitochondria. With pea leaf mitochondria oxidizing malate, inactivation of PDC was pH dependent corresponding to the production of pyruvate via malic enzyme. When pea leaf mitochondria oxidized succinate or glycine, PDC was inactivated. This inactivation was reversed by the addition of pyruvate. Reactivation by pyruvate was enhanced by the addition of thiamine pyrophosphate, as previously observed with nonrespiring mitochondria. These results indicate a major role for pyruvate in regulating the covalent modification of the PDC.

1 This research was supported in part by the Missouri Agriculture Experimental Station, National Science Foundation grant DMB-8506473 and the Food for the 21st Century Program. This is journal report 10468 from the Missouri Agricultural Experiment Station.




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Copyright © 1988 by the American Society of Plant Biologists