title: A comparison of the malate dehydrogenase of the propionic acid bacteria with the mammalian soluble and mitochondrial isoenzymes.
abstract: 1. Like the malate dehydrogenases of eucaryotic cells, the Propionibacterium shermanii enzyme is a dimer consisting of two 35,000 molecular weight subunits. 2. In electrophoretic behavior, resistance to substrate inhibition and stability to heating and dilution the P. shermanii MDH is more similar to the s-MDH than to the m-MDH of pig heart. 3. The P. shermanii MDH has a high turnover number (ca. 140,000) as well as Km values for both L-malate and oxalacetate which are four times higher than the mammalian isoenzymes. 4. A coupled assay for MDH using the malate-lactate transhydrogenase and diaphorase is described in which both substrates, L-malate and NAD, are regenerated.
mesh_terms: D000818:Animals; D007527:Isoenzymes / Q000032:analysis*; D008291:Malate Dehydrogenase / Q000032:analysis*; D008929:Mitochondria, Heart / Q000201:enzymology*; D011424:Propionibacterium / Q000201:enzymology*; D012995:Solubility; D013552:Swine
chemical_list: D007527:Isoenzymes; D008291:Malate Dehydrogenase