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- W137391888 abstract "Publisher Summary The regulation of yeast metabolism, in particular yeast gluconeogenesis, has been the object of study in several laboratories in the past few years. More recently, short-term experiments have revealed that under certain culture conditions this inactivation can be preceded by a very rapid and reversible phase in which about 50% of the activity is lost. During this reversible phase, an incorporation of phosphate into the enzyme has been observed. Addition of glucose to a yeast culture growing on a gluconeogenic carbon source causes an irreversible inactivation of FbPase. During this process, which takes place in about 1 hour, there is a proteolytic degradation of the enzyme. However, in some conditions, about 50% of the initial enzymatic activity is lost within 1 minute after the addition of glucose, the process being fully reversible in the absence of protein synthesis. The rapid inactivation of FbPase is fully reversible in the absence of protein synthesis and takes place without loss of antigenic material in yeast grown on a rich medium with glucose. When FbPase is inactivated in vivo by the addition of glucose, a phosphorylation of the protein occurs concomitantly. Incubation of purified FbPase with a cAMP-dependent kinase leads to a slow loss of activity. When the inactivation by protein kinase is performed, an incorporation of 32P into FbPase is observed that correlates well with the loss of activity." @default.
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- W137391888 date "1985-01-01" @default.
- W137391888 modified "2023-09-26" @default.
- W137391888 title "Regulation of Yeast Fructose-1,6-Bisphosphatase by Phosphorylation–Dephosphorylation" @default.
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- W137391888 doi "https://doi.org/10.1016/b978-0-12-152827-0.50020-7" @default.
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