Abstract
ABSTRACT The proteolytic system in yeast consists of at least 7 intracellular proteinases and 3 specific macromolecular proteinase inhibitors. The proteinases have been shown to play a role in the regulation of yeast enzymes. The following 4 types of proteolytic processes are discussed by which selected yeast enzymes might be regulated: 1) activation of inactive proforms of chitin synthase and carboxypepti dase Y by limited proteolysis; 2) activation of the inactive inhibitor complexes of the proteinases A and B and of carboxypeptidase Y by proteolytic degradation of the respective inhibitors; 3) in-activation of enzymes by proteolytic degradation as shown for the glucose-induced “catabolite inactivation” of cytoplasmic malate dehydrogenase and for the glucose starvation-promoted inactivation of NADP-dependent glutamate dehydrogenase; 4) irreversible glucose-effected decrease in the affinities of the galactose uptake system and the maltose uptake system for galactose and maltose, respectively.
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