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Simultaneous Oxidation of Glycine and Malate by Pea Leaf Mitochondria
Author(s) -
Griffin H. Walker,
David J. Oliver,
G. Sarojini
Publication year - 1982
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.70.5.1465
Subject(s) - glycine , malate dehydrogenase , mitochondrion , biochemistry , pisum , nad+ kinase , biology , chemistry , amino acid , enzyme
Mitochondria isolated from pea leaves (Pisum sativum L.) readily oxidized malate and glycine as substrates. The addition of glycine to mitochondria oxidizing malate in state 3 diminished the rate of malate oxidation. When glycine was added to mitochondria oxidizing malate in state 4, however, the rate of malate oxidation was either unaffected or stimulated. The reason both glycine and malate can be metabolized in state 4 appears to be that malate only used part of the electron transport capacity available in these mitochondria in this state. The remaining electron transport capacity was used by glycine, thus allowing both substrates to be oxidized simultaneously. This can be explained by differential use of two NADH dehydrogenases by glycine and malate and an increase in alternate oxidase activity upon glycine addition. These results help explain why photorespiratory glycine oxidation and its associated demand for NAD do not inhibit citric acid cycle function in leaves.

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