The effect of fructose 2,6-bisphosphate and AMP on the activity of phosphorylated and unphosphorylated fructose-1,6-bisphosphatase from rat liver
- 27 February 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 167 (2) , 203-209
- https://doi.org/10.1016/0014-5793(84)80127-1
Abstract
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 K 0.5 and V max, while the main effect of AMP was to lower V max. 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.Keywords
This publication has 19 references indexed in Scilit:
- Reciprocal regulation of fructose 1,6-bisphosphatase and phosphofructokinase by fructose 2,6-bisphosphate in swine kidneyLife Sciences, 1983
- The effect of fructose 2,6-bisphosphate on the reverse reaction kinetics of fructose 1,6-bisphosphatase from bovine liverBiochemical and Biophysical Research Communications, 1982
- Cyclic AMP-dependent phosphorylation of rat liver 6-phosphofructo 2-kinase/fructose 2,6-bisphosphataseBiochemical and Biophysical Research Communications, 1982
- Phosphofructokinase 2 the enzyme that forms fructose 2,6-bisphosphate from fructose 6-phosphate and ATPBiochemical and Biophysical Research Communications, 1981
- Fructose 1,6-bisphosphatase in rat liver cytosol: Activation after glucagon treatment in vivo and inhibition by fructose 2,6-bisphosphate in vitroBiochemical and Biophysical Research Communications, 1981
- Regulation of fructose 2,6-P2 concentration in isolated hepatocytesBiochemical and Biophysical Research Communications, 1981
- Evidence for a new activator of rat liver phosphofructokinaseBiochemical and Biophysical Research Communications, 1981
- Amino acid sequence at the phosphorylated site of rat liver fructose-1,6-diphosphatase and phosphorylation of a corresponding synthetic peptideBiochemical and Biophysical Research Communications, 1979
- Purification and properties of a phosphoprotein phosphatase from rat liverBiochimica et Biophysica Acta (BBA) - Enzymology, 1977
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976