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Open Access Green as soon as Postprint is submitted to ZB.
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)
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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Publication type
Article: Journal article
Document type
Scientific Article
ISSN (print) / ISBN
0006-291X
e-ISSN
1090-2104
Quellenangaben
Volume: 115,
Issue: 1,
Pages: 317-324
Publisher
Elsevier
Reviewing status
Peer reviewed
Institute(s)
Abteilung für Enzymchemie