ADPGlucose pyrophosphorylase: evidence for a lysine residue at the activator site of the Escherichia coli B enzyme.
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Adenosine Diphosphate Glucose↗
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Results for “Fructosephosphates”
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Control of pyruvate kinase activity by glucagon in isolated hepatocytes.
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Animals↗
Study on the regulatory role of fructose-1,6-diphosphate in the formation of AMP in rat skeletal muscle. A mechanism for synchronization of glycolysis and the purine nucleotide cycle.
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AMP Deaminase↗
On the stereospecific reduction of the aldolase-fructose 1,6 bisphosphate complex by NaBH4.
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Animals↗
A fluorimetric study of substrate and effector binding of D-ribulose-1,5-biphosphate carboxylase/oxygenase from spinach.
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Binding Sites↗
Binding of fructose-6-phosphate to phosphofructokinase from yeast.
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Allosteric Regulation↗
Avian heart fructose 1,6-bisphosphatase-an embryonic enzyme.
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Adenosine Monophosphate↗
Effects of AMP and Cibacron blue F3G-A on the fructose 6-phosphate binding of yeast phosphofructokinase.
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Adenosine Monophosphate↗
The reversal of inhibition of protein synthesis by double-stranded RNA in lysed rabbit reticulocytes with fructose 6-phosphate.
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Animals↗
Certain phosphorylated sugars can prevent the mRNA-induced inhibition of Met-tRNA f Met binding to initiation factor eIF-2.
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Animals↗
Synthesis of a stimulator of phosphofructokinase, most likely fructose 2,6-bisphosphate, from phosphoric acid and fructose 6-phosphoric acid.
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Animals↗
Effect of experimental diabetes on glycolytic intermediates and regulation of phosphofructokinase in rat lens.
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Adenine Nucleotides↗
Inorganic pyrophosphate: D-fructose-6-phosphate 1-phosphotransferase in mung beans and its activation by D-fructose 1,6-bisphosphate and D-glucose 1, 6-bisphosphate.
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Enzyme Activation↗
Partial purification of a rat liver enzyme that catalyzes the formation of fructose 2,6-bisphosphate.
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Adenosine Triphosphate↗
Phosphofructokinase 2: the enzyme that forms fructose 2,6-bisphosphate from fructose 6-phosphate and ATP.
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Adenosine Triphosphate↗
Fructose 2,6-bisphosphate as a contaminant of commercially obtained fructose 6-phosphate: effect on PPi:fructose 6-phosphate phosphotransferase.
Fructose 6-phosphate from several commercial sources was shown to be contaminated with fructose 2,6-bisphosphate. This contaminant was identified by its activation of PPi:fructose 6-phosphate phosphotransferase, extreme acid lability and behaviour on ion-exchange chromatography. The apparent kinetic properties of PPi:fructose 6-phosphate phosphotransferase from castor bean endosperm were considerably altered when contaminated fructose 6-phosphate was used as a substrate. Varying levels of fructose 2,6-bisphosphate in the substrate may account for differences that have been observed in the properties of the above enzyme from several plant sources.
Chromatography, Ion Exchange↗
Inhibition of rat liver phosphofructokinase-2 by phosphoenolpyruvate and ADP.
Phosphofructokinase-2 from rat liver is inhibited by phosphoenolpyruvate and ADP. Phosphoenolpyruvate reduces the maximum activity in respect to fructose-6-phosphate and ATP but does not give rise to complete inhibition of phosphofructokinase-2. ADP increases the apparent Michaelis constant of the enzyme for ATP and leaves the maximum activity in respect to ATP unchanged. The apparent Michaelis constant for fructose-6-phosphate is not influenced by ADP.
Adenosine Diphosphate↗
Enzyme concentration affects the allosteric behavior of yeast phosphofructokinase.
The influence of enzyme concentration on the kinetic behavior of yeast phosphofructokinase has been examined. A marked decrease in the ATP inhibition was observed when the enzyme activity was studied in permeabilized cells (in situ) as well as when the kinetic study was carried out with the purified yeast enzyme at a concentration of 120 micrograms/ml as compared to a 100-fold diluted enzyme. A similar result was obtained by adding polyethylene glycol either to a cell free extract or to the diluted pure enzyme to increase the local protein concentration. However, enzyme concentration had no significant effect on the fructose-6-P saturation curve. These results provide evidence that the allosteric behavior of yeast phosphofructokinase is affected by enzyme concentration.
Adenosine Triphosphate↗