Comparison of the kinetic behavior toward pyridine nucleotides of NAD+-linked dehydrogenases from plant mitochondria

Abstract

In this article we compare the kinetic behavior toward pyridine nucleotides (NAD+, NADH) of NAD+-malic enzyme, pyruvate dehydrogenase, isocitrate dehydrogenase, α-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.