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The effect of fructose-2,6-bisphosphate and AMP on unphosphorylated and phosphorylated fructose-1,6-bisphosphatase from rat liver
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (ek pia)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (ek pia)
1984 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 167, no 2, 203-209 p.Article in journal (Refereed) Published
Abstract [en]

Rat liver fructose-1,6-bisphosphatase was partially phosphorylated in vitro and separated into unphosphorylated and fully phosphorylated enzyme. The effects of fructose 2,6-bisphosphate and AMP on these two enzyme forms were examined. Unphosphorylated fructose-1,6-bisphosphatase was more easily inhibited by both effectors. Fructose 2,6-bisphosphate affected both K0.5 and Vmax, while the main effect of AMP was to lower Vmax. Fructose 2,6-bisphosphate and AMP together acted synergistically to decrease the activity of fructose-1,6-bisphosphatase, and since unphosphorylated and phosphorylated enzyme forms are affected differently, this might be a way to amplify the effect of phosphorylation.

Place, publisher, year, edition, pages
1984. Vol. 167, no 2, 203-209 p.
Keyword [en]
fructose-1, 6-bisphosphatase, fructose-1, 6-bisphosphate, AMP, chromatofocusing, regulatory phosphorylation, cAMP-dependent protein kinase
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-172459DOI: 10.1016/0014-5793(84)80127-1OAI: oai:DiVA.org:uu-172459DiVA: diva2:514721
Available from: 2012-04-10 Created: 2012-04-10 Last updated: 2017-12-07Bibliographically approved

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