| 16667685 |
Pascal N, Dumas R, Douce R: Comparison of the Kinetic Behavior toward Pyridine Nucleotides of NAD-Linked Dehydrogenases from Plant Mitochondria. Plant Physiol. 1990 Sep;94(1):189-193.
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. |
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