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Metabolism and Enzymology

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

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, -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.

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