Glucose-induced degradation of yeast fructose-1,6-bisphosphatase requires additional triggering events besides protein phosphorylation
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منابع مشابه
Phosphorylation and inactivation of yeast fructose-1,6-bisphosphatase by cyclic AMP-dependent protein kinase from yeast.
Purified fructose-1,6-bisphosphatase from Saccharomyces cerevisiae was phosphorylated in vitro by purified yeast cAMP-dependent protein kinase. Maximal phosphorylation was accompanied by an inactivation of the enzyme by about 60%. In vitro phosphorylation caused changes in the kinetic properties of fructose-1,6-bisphosphatase: 1) the ratio R(Mg2+/Mn2+) of the enzyme activities measured at 10 mM...
متن کاملInactivation and phosphorylation of yeast fructose 1,6-bisphosphatase.
FBPase* from Saccharomyces cerevisiae is a highly regulated enzyme. Repression of its synthesis by sugars (Gancedo et al., 1967) and allosteric inhibition by AMP (Gancedo et al., 1965) have been documented. Moreover, glucose can inactivate the enzyme. In certain conditions the loss of enzymic activity is paralleled by a loss of cross-reacting material against FBPase antibodies (Funayama et al.,...
متن کاملAmino acid sequence of the phosphorylation site of yeast (Saccharomyces cerevisiae) fructose-1,6-bisphosphatase.
Fructose-1,6-bisphosphatase from the yeast Saccharomyces cerevisiae has properties similar to other gluconeogenic fructose-1,6-bisphosphatases, but an unusual characteristic of the yeast enzyme is that it can be phosphorylated in vitro by cAMP-dependent protein kinase. Phosphorylation also occurs in vivo, presumably as part of a signalling mechanism for the enzyme's degradation. To probe the st...
متن کاملInactivation of yeast fructose-1,6-bisphosphatase. In vivo phosphorylation of the enzyme.
Incorporation of 32P into yeast fructose-1,6-bisphosphatase (EC 3.1.3.11) was observed after addition of glucose to a cell suspension incubated with (32P)orthophosphoric acid. The 32P counts were coincident with the enzyme band when immunoprecipitates were subjected to sodium dodecyl sulfate disc gel electrophoresis. The incorporation of phosphate was associated with a decrease in enzyme activi...
متن کاملPhosphorylation of rat hepatic fructose-1,6-bisphosphatase and pyruvate kinase.
Fructose-1,6-bisphosphatase from rat liver was phosphorylated with cyclic AMP-dependent protein kinase and [gamma-32P]ATP. Brief exposure of the 32P-labeled enzyme to trypsin removed all radioactivity from the enzyme core and produced a single-labeled peptide. The partial sequence of the 17-amino acid peptide was found to be Ser-Arg-Pro-Ser(P)-Leu-Pro-Leu-Pro-(Ser2, Glx2, Pro2, Leu, Arg2). The ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1987
ISSN: 0014-5793
DOI: 10.1016/0014-5793(87)80703-2