Inactivation of Yeast Enzymes by Proteinase A and B and Carboxypeptidase Y from Yeast
- 1 January 1976
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 357 (1) , 735-740
- https://doi.org/10.1515/bchm2.1976.357.1.735
Abstract
Changes in the activities of 15 enzymes during incubation of a crude yeast extract with the purified yeast proteinases A and B, and carboxypeptidase Y, respectively, were measured. The action spectrum of the 3 proteinases on the enzymes measured differs significantly, increasing or decreasing their activities or having no effect. Incubation of purified cytoplasmic malate dehydrogenase or purified mitochondrial malate dehydrogenase (Saccharomyces cerevisiae) with proteinases A and B results in selective inactivation of the cytoplasmic enzyme, whereas the mitochondrial activity is not affected. Carboxypeptidase Y has no effect on the activity of either dehydrogenase. The results support the idea of selective proteolysis as the mechanism of the earlier observed inactivation of cytoplasmic malate dehydrogenase, initiated by the addition of glucose to intact yeast cells grown on acetate as C source (glucose effect).This publication has 17 references indexed in Scilit:
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