Inhibition of fructose-1,6-bisphosphatase by fructose 2,6-biphosphate.
Proceedings of the National Academy of SciencesPublished 1 May 1981Open access
Emile Van Schaftingen, H G Hers
Citations256
SJR quartileQ1
SJR score3.41
SNIP2.38
Generate an AI Snapshot to get a quick, structured summary of this paper.
Study Snapshot
ObjectiveStudy objective
MethodsResearch methodology
PopulationPopulation studied
Sample sizeSample sizes
OutcomesStudy outcomes here
ResultsStudy results comes here
LimitationsResearch study limitations comes here
A concise AI-generated summary of the paper will appear here once you click Generate AI Snapshot.
TL;DR
Fructose 2,6-bisphosphate, a known powerful stimulator of phosphofructokinase, was found to inhibit, at micromolar concentrations, liver and muscle fructose-1-6-biphosphate (D-fructose-1, 6-bisPhosphate 1-phosphohydrolase, EC 3.3.1.11).
Abstract
Fructose 2,6-bisphosphate, a known powerful stimulator of phosphofructokinase [Van Schaftingen, E., Hue, L. & Hers, H.-G. (1980) Biochem. J. 192, 897-901] was found to inhibit, at micromolar concentrations, liver and muscle fructose-1,6-biphosphate (D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11). The main characteristics of this inhibition are that (i) it is much stronger at low than at high substrate concentrations, (ii) it changes the substrate saturation curve from almost hyperbolic to sigmoidal, and (iii) it is synergistic with the inhibition by AMP. This inhibition may play an important role in the stimulation of gluconeogenesis by glucagon, because this hormone is known to decrease the concentration of fructose 2,6-bisphosphate in the liver [Van Schaftingen, E., Hue, L. & Hers, H.-G. (1980) Biochem. J. 192, 887-895].
Keywords
MedicineBiochemistry, Genetics and Molecular Biology
Journal of Biological ChemistryAllosteric Inhibition of Rat Liver Fructose 1,6-Diphosphatase by Adenosine 5'-Monophosphate
518 Citations1965Kazuhisa Taketa, Burton M. Pogell
Three possible mechanisms for the regulation of liver fructose 1,6-diphosphatase activity under physiological conditions are reported, including the specific and reversible inhibition by adenosine 5’-monophosphate, the reversible inhibition of the enzyme by substrate at concentrations greater than 0.1 mM, and the reversible inactivation of fructose1,6diph phosphatase by reaction with ATP or ADP.
Biochemical JournalFructose 2,6-bisphosphate, the probably structure of the glucose- and glucagon-sensitive stimulator of phosphofructokinase
315 Citations1980Emile Van Schaftingen, Louis Hue +1 more
Biochemical JournalControl of the fructose 6-phosphate/fructose 1,6-bisphosphate cycle in isolated hepatocytes by glucose and glucagon. Role of a low-molecular-weight stimulator of phosphofructokinase
211 Citations1980Emile Van Schaftingen, Louis Hue +1 more
The activity of phosphofructokinase present in a liver Sephadex filtrate was increased by a low-molecular-weight effector, which could be isolated from a liver extract by ultrafiltration, gel filtration or heat treatment, but was rapidly destroyed in trichloroacetic acid, even in the cold.
Journal of Biological ChemistryInhibition of Glucagon Effects in Perfused Rat Liver by (+)Decanoylcarnitine
141 Citations1969John Williamson, Edward T. Browning +2 more
The results are interpreted as indicating that either other modulators, not measured in the present experiments, affect the activity of these enzymes, or that the concentrations of acetyl-CoA and citrate increased specifically in the mitochondrial and cytosolic compartments, respectively, without appreciably affecting the total tissue contents.
Journal of Biological ChemistryHormonal control of [14C]glucose synthesis from [U-14C]dihydroxyacetone and glycerol in isolated rat hepatocytes
107 Citations1976S.J. Pilkis, J. P. Riou +1 more
Estimates of the steady state levels of intermediary metabolites and flux rates suggested that glucagon activated conversion of fructose diphosphate to fructose 6-phosphate and suppressed conversion of phosphoenolpyruvate to pyruvates, which may reduce recycling in the pathway of gluconeogenesis from major physiological substrates.
Biochemical and Biophysical Research CommunicationsSynthesis of a stimulator of phosphofructokinase, most likely fructose 2,6-bisphosphate, from phosphoric acid and fructose 6-phosphoric acid
95 Citations1980Emile Van Schaftingen, H G Hers
A phosphoric ester having all the properties of the natural stimulator of phosphofructokinase recently isolated from rat liver and tentatively identified as fructose 2,6-bisphosphate is formed, indicating that no compounds other than phosphate and fructose 6-phosphates enter into the structure of the stimulator.
Journal of Biological ChemistryInfluence of Glucagon on the Metabolism of Xylitol and Dihydroxyacetone in the Isolated Perfused Rat Liver
87 Citations1973James B. Blair, David E. Cook +1 more
The observations reported in this communication suggest that the effect of glucagon on gluconeogenesis and glycolysis is the result of a complex interaction rather than regulation of one particular enzyme of the gluconeogenic-glycolytic pathway.
Biochemical JournalStudy of the fructose 6-phosphate/fructose 1,6-bi-phosphate cycle in the liver <i>in vivo</i>
83 Citations1980Emile Van Schaftingen, Louis Hue +1 more
The main factors that appear to be responsible for the very large changes in recycling observed in various experimental conditions are the concentrations of fructose 1,6-bisph phosphate and of fructose 6-phosphate and also the affinity of phosphofructokinase for fructose 6 -phosphates and the concentration of nucleotides.
Archives of Biochemistry and BiophysicsThe purification of properties of rat liver fructose 1,6-bisphosphatase
76 Citations1976Gopi A. Tejwani, Fábio O. Pedrosa +2 more
Fructose 1,6-bisphosphatase has been isolated in homogeneous form from rat liver by a simple and convenient procedure, including adsorption on carboxymethyl cellulose and substrate elution, and reaction to antibody to the purified enzyme shows some similarity to that of the rabbit liver enzyme, with a blocked NH 2 -terminus and leucine, rather than alanine, as the COOH-terminal residue.
Biochemical JournalSYNTHESIS OF <scp>d</scp>-FRUCTOPYRANOSE 2-PHOSPHATE AND <scp>d</scp>-FRUCTOFURANOSE 2-PHOSPHATE
39 Citations1963HG PONTIS, C. R. Fischer