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Purwin, C. ; Leidig, F. ; Holzer, H.

Cyclic AMP-dependent phosphorylation of fructose-1,6-bisphosphatase in yeast.

Biochem. Biophys. Res. Commun. 107, 1482-1489 (1982)

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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.

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Previous in vivo experiments have shown that simultaneously with the glucose-induced inactivation of yeast fructose-1,6-bisphosphatase a phosphorylation of serine residues of the enzyme occurs. The inactivation of fructose-1,6-bisphosphatase dependent on ATP, Mg++ and cyclic AMP is now demonstrated in a cell-free yeast extract suggesting the existence of a cyclic AMP-dependent fructose-1,6-bisphosphatase kinase. When glucose is added to intact yeast cells within 30 sec the cyclic AMP concentration increases from 0.7 to 3 nmol per g wet weight. This observation suggests that upon addition of glucose to yeast cells cyclic AMP functions as the mediating signal for the protein kinase catalyzed phosphorylation of fructose-1,6-bisphosphatase. The levels of glucose-6-phosphate and fructose-6-phosphate also show a transient rise with a maximum 15 to 30 sec after the addition of glucose to yeast cells, i.e. shortly before the observed increase of the cyclic AMP concentration. Thus, the sugar phosphates may function as allosteric effectors which stimulate adenylate cyclase and/or inhibit cyclic AMP phosphodiesterase thereby leading to a transient rise of the cyclic AMP levels, which in turn may be the signal for the phosphorylation of fructose-1,6-bisphosphatase.

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