Catabolite inactivation of fructose 1,6-bisphosphatase and cytoplasmic malate dehydrogenase in yeast.
Catabolite inactivation of fructose 1,6-bisphosphatase and cytoplasmic malate dehydrogenase was studied using the protease-deficient and vacuole-defective yeast strain pep4-3. The catabolite inactivation of fructose 1,6-bisphosphatase in pep4-3 was found to have a normal first inactivation step but with a defective second proteolytic step. In contrast, catabolite inactivation of cytoplasmic malate dehydrogenase was normal in pep4-3. These results suggest that the proteolytic pathways utilized in the hydrolysis of the two enzymes may be different and that proteolysis of fructose 1,6-bisphosphatase may require functional vacuoles while proteolysis of cytoplasmic malate dehydrogenase may not.
Funaguma
T
T
Toyoda
Y
Y
Sy
J
J
D003593:Cytoplasm / Q000201:enzymology; D006597:Fructose-Bisphosphatase / Q000378:metabolism*; D008291:Malate Dehydrogenase / Q000378:metabolism*; D008928:Mitochondria / Q000201:enzymology; D010447:Peptide Hydrolases / Q000172:deficiency; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics / Q000648:ultrastructure; D014617:Vacuoles / Q000201:enzymology
D008291:Malate Dehydrogenase; D006597:Fructose-Bisphosphatase; D010447:Peptide Hydrolases