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During glycine oxidation by spinach leaf mitochondria, oxygen consumption showed a strong and transient inhibition upon addition of oxaloacetate or aspartate plus alpha-ketoglutarate. During the course of the inhibition, aspartate and alpha-ketoglutarate were stoichiometrically transformed into malate and glutamate.It is concluded that oxaloacetate formed by transamination is reduced by the malate dehydrogenase, which allows the regeneration of NAD(+) for glycine oxidation and, thus, by-passes the respiratory chain. Efficiency of a malate-glutamate/aspartate-alpha-ketoglutarate shuttle upon illumination and under in vivo conditions is discussed.

plant physiology

Role of Glutamate-oxaloacetate Transaminase and Malate Dehydrogenase in the Regeneration of NAD<sup>+</sup> for Glycine Oxidation by Spinach leaf Mitochondria

Role of Glutamate-oxaloacetate Transaminase and Malate Dehydrogenase in the Regeneration of NAD+ for Glycine Oxidation by Spinach leaf Mitochondria

Role of Glutamate-oxaloacetate Transaminase and Malate Dehydrogenase in the Regeneration of NAD⁺ for Glycine Oxidation by Spinach leaf Mitochondria