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

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

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 super(32)P into fructose-1,6-bisphosphatase could be demonstrated only...

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Veröffentlicht in:Biochemical and biophysical research communications 1983-01, Vol.115 (1), p.317-324
Hauptverfasser: Pohlig, G, Wingender-Drissen, R, Noda, T, Holzer, H
Format: Artikel
Sprache:eng
Schlagworte:
AMP
cyclic AMP
fructose-2,6-diphosphate
fructose-bisphosphatase
protein kinase
yeasts
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Zusammenfassung: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 super(32)P 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 mu M fructose-2,6-bisphosphate and inhibited by 1 mM 5'-AMP.
ISSN:0006-291X