Isoenzyme der malatdehydrogenase und ihre regulation in Saccharomyces cerevisiae

Abstract

Abstract 1. 1. From Saccharomyces cerevisiae, incubated on a glucose-free medium with acetate as the only carbon source, two different malate dehydrogenases ( l -malate: NAD+ oxidoreductase, EC 1.1.1.37) have been isolated by DEAE-cellulose ion-exchange chromatography. One of these enzymes was only found in the mitochondria and is called enzyme A or m-malate dehydrogenase; the other enzyme was found in the extramitochondrial c-space and is called enzyme B or c-malate dehydrogenase. At present it cannot be decided whether m-malate dehydrogenase also exists in the c-space or leaks when the mitochondria are injured. 2. 2. The reaction velocity plotted against the concentration of oxaloacetic acid showed a characteristic substrate inhibition in the case of m-malate dehydrogenase In contrast, c-malate dehydrogenase showed no substrate inhibition. This difference corresponds to the behaviour of m-malate dehydrogenase and c-malate dehydrogenase from liver. 3. 3. In yeast grown on glucose only m-malate dehydrogenase could be found, but after incubating the cells on acetate as the sole carbon source, both m-malate dehydrogenase and c-malate dehydrogenase were found. In reference to earlier experiments concerning the regulation of malate dehydrogenase activity in yeast, it is concluded that a repression of c-malate dehydrogenase synthesis by glucose occurs. This regulating mechanism is useful for the cell, because in the glycoxylate cycle c-malate dehydrogenase participates in the gluconeogenesis from acetate or ethanol. This enzyme is not necessary when glucose is in the medium.