Aggregation states of mitochondrial malate dehydrogenase

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...

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,...

Physicochemical properties of pig and horse heart mitochondrial malate dehydrogenase.

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 ...

Genetically induced subcellular mislocation of Neurospora mitochondrial malate dehydrogenase.

Among 60 ultraviolet-induced missense mutations of the structural genes that code for mitochondrial malate dehydrogenase (M-MDH, EC 1.1.1.37) of Neurospora crassa, two enzyme phenotypes are observed. In a previously described class (C-mutants), M-MDH is malfunctional because of an abnormal conformation induced by association with mitochondria. We describe here a second class (K-mutants) in whic...