Catabolite inactivation of fructose 1,6-bisphosphatase and cytoplasmic malate dehydrogenase in yeast

1985 ◽  
Vol 130 (1) ◽  
pp. 467-471 ◽  
Author(s):  
T. Funaguma ◽  
Y. Toyoda ◽  
J. Sy
Keyword(s):  
Malate Dehydrogenase ◽  
Catabolite Inactivation ◽  
Fructose 1,6 Bisphosphatase

scholarly journals Catabolite inactivation of fructose-1,6-bisphosphatase in yeast is mediated by the proteasome

FEBS Letters ◽  
1994 ◽  
Vol 349 (2) ◽  
pp. 270-274 ◽  
Author(s):  
Stefan M. Schork ◽  
Gisela Bee ◽  
Michael Thumm ◽  
Dieter H. Wolf
Keyword(s):  
Catabolite Inactivation ◽  
Fructose 1,6 Bisphosphatase

scholarly journals Glucose-induced inactivation of mitochondrial enzymes in the yeast Saccharomyces cerevisiae

1981 ◽  
Vol 198 (2) ◽  
pp. 281-287 ◽  
Author(s):  
M Takeda
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Malate Dehydrogenase ◽  
Mitochondrial Enzymes ◽  
Yeast Saccharomyces Cerevisiae ◽  
Cytoplasmic Proteins ◽  
Fructose 1,6 Bisphosphatase ◽  
Specific Activities

1. Addition of glucose induced an inactivation of mitochondrial enzymes in the yeast Saccharomyces cerevisiae containing normal mitochondrial particles. 2. The glucose-induced inactivation of mitochondrial enzymes was inhibited by the presence of cycloheximide. 3. Pepstatin also inhibited the inactivation, but phenylmethanesulphonyl fluoride accelerated the inactivation. 4. The specific activities of fructose 1,6-bisphosphatase and cytoplasmic malate dehydrogenase were decreased on the exposure to glucose, as well as those of the mitochondrial enzymes. However, the glucose-induced inactivation of cytoplasmic enzymes was not inhibited by the presence of pepstatin. 5. The specific activities of hexokinase and phosphofructokinase, which are cytoplasmic enzymes were increased by the addition of glucose, and this effect was not affected by pepstatin. 6. Addition of glucose resulted in an increase in the synthesis of proteins of the mitochondria and the cytosol, and simultaneously in degradation of these mitochondrial and cytoplasmic proteins.

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