Abstract
NADP-glutamate dehydrogenase (NADP-GDH) from Saccharomyces cerevisiae has a lower activity in yeast grown on glutamate as nitrogen source than when grown on ammonium. With the use of the immunotitration method, it was found that the difference in activity was parallel to the difference in immunoprecipitable material. By isotope incorporation studies, it was established that the decrease in NADP-glutamate dehydrogenase levels in glutamate-grown cells was brought about by an increase in the degradation rate and a decrease in the synthesis constant of the enzyme. The degradation rate of NADP-glutamate dehydrogenase is further increased in carbon-starved cells. The possible role of internal metabolites in modulating NADP-glutamate dehydrogenase degradation is discussed.
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