Light and Acetate Regulate a Mitochondrial Malate Dehydrogenase

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Regulation of Mitochondrial Malate Dehydrogenase

The effect of citrate on the structure and function of porcine heart mitochondrial malate dehydrogenase (EC 1.1.1.37) has been characterized. The native dimeric form of this enzyme is specifically activated by citrate in the NAD’ -+ NADH direction and inhibited by citrate in the NADH -+ NAD’ direction. It is proposed that citrate is bound at a regulatory site that is distinct from the catalytic...

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Subunit Interactions in Mitochondrial Malate Dehydrogenase

The pH-dependent dissociation of porcine heart mitochondrial malate dehydrogenase (t-malate:NAD+ oxidoreductase, EC 1.1.1.37) has been more extensively characterized. "he native, dimeric form of the enzyme (Mr = 70,000) which exists at pH 7.5 has previously been shown to dissociate into its constituent subunits (Mr = 35,000) at pH 5.0 (Bleile, D. M., Schulz, R. A., Gregory, E. M., and Harrison,...

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Tissue distribution of microbody, mitochondrial, and soluble malate dehydrogenase isoenzymes.

Many tissues which have been investigated have at least two malate dehydrogenase isoenzymes. One is an organelle form localized in mitochondrial fractions whereas the other does not appear to associate with organelles sedimenting after high speed centrifugation (17). Spinach leaf tissue has an additional malate dehydrogenase isoenzyme localized in the peroxisome or leaf microbody fraction (12, ...

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Interaction of mitochondrial malate dehydrogenase monomer with phospholipid vesicles.

The association between bovine and porcine mitochondrial malate dehydrogenase (EC 1.1.1.37) and phospholipid vesicles was investigated. At concentrations at which malate dehydrogenase exists as a dimer, entrapment within the aqueous compartment but not binding of the 14C-labelled enzyme was observed. The dissociated enzyme was labile to moderate heat and to p-chloromercuribenzoate, but in both ...

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ژورنال

عنوان ژورنال: Plant Physiology

سال: 1987

ISSN: 0032-0889,1532-2548

DOI: 10.1104/pp.85.1.124