Plant Physiol. Drug Metab Dispos
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Plant Physiology 94:189-193 (1990)
© 1990 American Society of Plant Biologists

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Metabolism and Enzymology

Comparison of the Kinetic Behavior toward Pyridine Nucleotides of NAD+-Linked Dehydrogenases from Plant Mitochondria

Nadine Pascal, Renaud Dumas1 and Roland Douce

Laboratoire de Physiologie Cellulaire Vegetale, Centre d'Etudes Nucléaires de Grenoble et Université Joseph Fourier, 85X, F-38041 Grenoble-Cedex, France, Unité Associée au Centre National de la Recherche Scientifique No. 576, Département de Recherche Fondamentale, Centre d'Etudes Nucléaires de Grenoble et Université Joseph Fourier, 85X, F-38041 Grenoble-Cedex, France

In this article we compare the kinetic behavior toward pyridine nucleotides (NAD+, NADH) of NAD+-malic enzyme, pyruvate dehydrogenase, isocitrate dehydrogenase, {alpha}-ketoglutarate dehydrogenase, and glycine decarboxylase extracted from pea (Pisum sativum) leaf and potato (Solanum tuberosum) tuber mitochondria. NADH competitively inhibited all the studied dehydrogenases when NAD+ was the varied substrate. However, the NAD+-linked malic enzyme exhibited the weakest affinity for NAD+ and the lowest sensitivity for NADH. It is suggested that NAD+-linked malic enzyme, when fully activated, is able to raise the matricial NADH level up to the required concentration to fully engage the rotenone-resistant internal NADH-dehydrogenase, whose affinity for NADH is weaker than complex I.

1 Present address: Laboratoire mixte CNRS/Rhône-Poulenc, Unité Associée au Centre National de la Recherche Scientifique No. UM41, Rhône-Poulenc Agrochimie, 14-20 rue Pierre Baizet, 69009 Lyon, France.




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M. A. Tronconi, H. Fahnenstich, M. C. Gerrard Weehler, C. S. Andreo, U.-I. Flugge, M. F. Drincovich, and V. G. Maurino
Arabidopsis NAD-Malic Enzyme Functions As a Homodimer and Heterodimer and Has a Major Impact on Nocturnal Metabolism
Plant Physiology, April 1, 2008; 146(4): 1540 - 1552.
[Abstract] [Full Text] [PDF]


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Copyright © 1990 by the American Society of Plant Biologists