Reversible inactivation of d-fructose 1,6-diphosphatase by adenosine triphosphate and cyclic 3′, 5′-adenosine monophosphate

Mendicino, Joseph; Beaudreau, Charles A.; Bhattacharyya, Rabindra N.

doi:10.1016/0003-9861(66)90050-6

Cited by 35 publications

(8 citation statements)

References 18 publications

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“…This observation has been further studied and it has been reported that incubation with ATP or ADP causes an inactivation of rabbit liver Fru-P,ase that develops slowly and can be reversed or prevented by a number of chelating agents, such as 3-P-glycerate, EDTA, pyrophosphate, citrate, oxaloacetate, phosphate Taketa et al, 1971), and oleate (Carlson et al, 1973). This observation has been confirmed by a number of other workers who have reported that swine kidney Fru-P,ase (Mendicino et al, 1966;Kratowich and Mendicino, 1970) and rabbit muscle Fru-P,ase (Fu and Kemp, 1973) are inactivated by ADP and ATP. It has been suggested that the reversal of the ADP and ATP inactivation by 3-P-glycerate may contribute to regulation of the activity of the enzyme Taketa et al, 1971).…”

Section: Inhibition By Ampsupporting

confidence: 70%

Regulation of Fructose‐Bisphosphatase Activity

Tejwani

1983

Advances in Enzymology - And Related Areas of Molecular Biology

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Section: Inhibition By Ampsupporting

confidence: 70%

Regulation of Fructose‐Bisphosphatase Activity

Tejwani

1983

Advances in Enzymology - And Related Areas of Molecular Biology

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“…Lme, 1967), has a high affinity for its However, ATP as well as citrate appeared to cause tor, AMP (K, is 4 x 10-8M at 0C). some inhibition of fructose diphosphatase activity, other systems (Taketa & Pogell, a finding also reported with the pig kidney enzyme & Hochachka, 1969a), inhibition of (Mendocino, Beaudreau & Bhattacharyan, 1966) enzyme by AMP is sensitive to and the bacterium Acinetobacter (Mukkada & Bell, Pig. 3). Thus as temperature is 1969).…”

Section: Resultsmentioning

confidence: 62%

Temperature and the regulation of enzyme activity in poikilotherms. Regulatory properties of fructose diphosphatase from muscle of the Alaskan king-crab

Behrisch

1971

Biochemical Journal

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1. The properties of fructose diphosphatase from skeletal muscle of the Alaskan king-crab (Paralithodes camtschatica) were examined over the physiological temperature range of the animal. 2. King-crab muscle fructose diphosphatase is first activated by Na(+) and NH(4) (+) and is then partially inhibited by these cations at concentrations higher than 10mm at 0 degrees , 8 degrees and 15 degrees C. Enzyme activity is stimulated by K(+) at 0 degrees C, but is curtailed at 8 degrees C and 15 degrees C, an effect that could render rate independent of temperature. 3. Affinity for substrate increases with decreasing temperature; below the temperature of acclimatization, K(m) for fructose 1,6-diphosphate increases, resulting in a complex U-shaped temperature-K(m) curve. 4. King-crab muscle fructose diphosphatase is inhibited by low concentrations of AMP. As with enzymes of other poikilotherms, inhibition by AMP is sensitive to temperature; the enzyme is least sensitive to inhibition by AMP near the temperature of acclimatization. 5. The affinity of fructose diphosphatase for fructose 1,6-diphosphate is enhanced by phosphoenolpyruvate, and this activation is temperature-sensitive; 0.5mm-phosphoenolpyruvate causes a sevenfold decrease in K(m) for fructose 1,6-diphosphate at 15 degrees C but a 25-fold decrease at 0 degrees C. 6. Phosphoenolpyruvate appears to decrease the affinity of king-crab muscle fructose diphosphatase for AMP at low temperature, whereas at the higher temperature it appears to enhance inhibition by AMP. Phosphoenolpyruvate was not observed to cause a reversal of inhibition of fructose diphosphatase activity by AMP. The identification of phosphoenolpyruvate as an activator of a rate-limiting step in gluconeogenesis permits the suggestion of a coupling of the controlling mechanisms of several steps in the glycolytic and gluconeogenic chains. 7. These findings suggest mechanisms for the maintenance and regulation of control of fructose diphosphatase activity in king-crab skeletal muscle at low temperature and under conditions that favour concomitant activity of phosphofructokinase.

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“…The enzyme was not -ffected by any of the following metabolites tested: glucose 1-phosphate, glucose 6-phosphate, fructose 6-phosphate, dihydroxyacetone phosphate, 2-phosphoglycerate, pyruvate, lactate, phosphoenolpyruvate, ATP, oxaloacetate, citrate, isocitrate, asparagine, glutamate and NADH. Concentrations of ATP higher than 0-1 mm appeared to cause some inactivation of FDPase activity, a phenomenon also observed in swine kidney FDPase (Mendocino, Beaudreau & Bhattacharyan, 1966). A further experiment was attempted in which the pH of the reaction mixture was increased to 8-5.…”

Section: Resultsmentioning

confidence: 91%

Temperature and the regulation of enzyme activity in poikilotherms. Fructose diphosphatase from migrating salmon

Behrisch

1969

Biochemical Journal

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1. The calculated energy charge of the liver cell from migrating salmon is very low (0.464), in keeping with the extended starvation and high rates of muscular and biosynthetic activity of these organisms. 2. Affinity of fructose 1,6-diphosphatase for substrate increases with a decrease in temperature. 3. Arrhenius plots of the saturation kinetics are complex and suggest an interconversion of one or more forms of the enzyme; this interconversion is dependent on the identity of the cofactor. 4. Affinity of salmon fructose 1,6-diphosphatase for its allosteric inhibitor (AMP) is lower than in other fructose 1,6-diphosphatases and this enzyme-AMP interaction is largely insensitive to temperature. The functional significance of diminished AMP-sensitivity is that it allows normal or high fructose 1,6-diphosphatase activity during a low energy charge. 5. These findings suggest mechanisms for the maintenance of high rates of gluconeogenesis in salmon during spawning migration.

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Reversible inactivation of d-fructose 1,6-diphosphatase by adenosine triphosphate and cyclic 3′, 5′-adenosine monophosphate

Cited by 35 publications

References 18 publications

Regulation of Fructose‐Bisphosphatase Activity

Regulation of Fructose‐Bisphosphatase Activity

Temperature and the regulation of enzyme activity in poikilotherms. Regulatory properties of fructose diphosphatase from muscle of the Alaskan king-crab

Temperature and the regulation of enzyme activity in poikilotherms. Fructose diphosphatase from migrating salmon

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