The effect of fructose-2,6-bisphosphate and AMP on unphosphorylated and phosphorylated fructose-1,6-bisphosphatase from rat liver
1984 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 167, no 2, 203-209 p.Article in journal (Refereed) Published
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.
fructose-1, 6-bisphosphatase, fructose-1, 6-bisphosphate, AMP, chromatofocusing, regulatory phosphorylation, cAMP-dependent protein kinase
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:uu:diva-172459DOI: 10.1016/0014-5793(84)80127-1OAI: oai:DiVA.org:uu-172459DiVA: diva2:514721