PuSH - Publication Server of Helmholtz Zentrum München: Cyclic AMP and fructose-2,6-bisphosphate stimulated in vitro phosphorylation of yeast fructose-1,6-bisphosphatase.

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Pohlig, G.* ; Wingender-Drissen, R.* ; Noda, T.* ; Holzer, H.

Cyclic AMP and fructose-2,6-bisphosphate stimulated in vitro phosphorylation of yeast fructose-1,6-bisphosphatase.

Biochem. Biophys. Res. Commun. 115, 317-324 (1983)

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Phosphorylation of purified yeast fructose-1,6-bisphosphatase was studied using purified preparations from yeast of two different cyclic AMP-independent protein kinases and a cyclic AMP-dependent protein kinase. Incorporation of 32P into fructose-1,6-bisphosphatase could be demonstrated only with the cyclic AMP-dependent protein kinase. Phosphorylation of fructose-1,6-bisphosphatase was stimulated by 3 μM fructose-2,6-bisphosphate and inhibited by 1 mM 5′-AMP.

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