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

EtiennePascal Journet | Zendy; Michel Neuburger | Zendy; Roland Douce | Zendy

Open Access

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

Author(s) -

EtiennePascal Journet,

Michel Neuburger,

Roland Douce

Publication year - 1981

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.67.3.467

Subject(s) - spinach , citrate synthase , malate dehydrogenase , nad+ kinase , glycine , biochemistry , transaminase , dehydrogenase , mitochondrion , glutamate dehydrogenase , chemistry , biology , enzyme , glutamate receptor , amino acid , receptor

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.

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