The inhibition of skeletal-muscle fructose 1,6-diphosphatase by adenosine monophosphate

Opie, LH; Newsholme, E. A.

doi:10.1042/bj1040353

Cited by 52 publications

(27 citation statements)

References 12 publications

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“…As shown in Table 1, it was necessary to use the crude extract for assay of PFK activity because the enzyme from some muscles is partially sedimented after centrifugation at 10000g and 114000g (in the ionic extraction medium). The values presented in a preliminary communication (Opie & Newsholme, 1965) were based on assays of the 114 OOOg supernatant, which explains why those activities are much lower than those now reported.…”

Section: Resultsmentioning

confidence: 56%

“…This investigation showed that phosphoenolpyruvate carboxykinase [GTP-oxaloacetate carboxy-lyase (transphosphorylating), EC 4.1.1.32] was present in white muscle, and, moreover, that the variation in its activity between various muscles corresponded to that of FDPase. A preliminary report of some of these results has been published (Opie & Newsholme, 1965 Mansour, 1965). …”

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confidence: 99%

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The activities of fructose 1,6-diphosphatase, phosphofructokinase and phosphoenolpyruvate carboxykinase in white muscle and red muscle

Opie¹,

Newsholme²

1967

Biochemical Journal

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354

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1. The activities of fructose 1,6-diphosphatase were measured in extracts of muscles of various physiological function, and compared with the activities of other enzymes including phosphofructokinase, phosphoenolpyruvate carboxykinase and the lactate-dehydrogenase isoenzymes. 2. The activity of phosphofructokinase greatly exceeded that of fructose diphosphatase in all muscles tested, and it is concluded that fructose diphosphatase could not play any significant role in the regulation of fructose 6-phosphate phosphorylation in muscle. 3. Fructosediphosphatase activity was highest in white muscle and low in red muscle. No activity was detected in heart or a deep-red skeletal muscle, rabbit semitendinosus. 4. The lactate-dehydrogenase isoenzyme ratio (activities at high and low substrate concentration) was measured in various muscles because a low ratio is characteristic of muscles that are more dependent on glycolysis for their energy production. As the ratio decreased the activity of fructose diphosphatase increased, which suggests that highest fructose-diphosphatase activity is found in muscles that depend most on glycolysis. 5. There was a good correlation between the activities of fructose diphosphatase and phosphoenolpyruvate carboxykinase in white muscle, where the activities of these enzymes were similar to those of liver and kidney cortex. However, the activities ofpyruvate carboxylase and glucose 6-phosphatase were very low in white muscle, thereby excluding the possibility of gluconeogenesis from pyruvate and lactate. 6. It is suggested that the presence of fructose diphosphatase and phosphoenolpyruvate carboxykinase in white muscle may be related to operation of the o-glycerophosphate-dihydroxyacetone phosphate and malate-oxaloacetate cycles in this tissue.The enzyme PFK$ (ATP-D-fructose 6-phosphate 1-phosphotransferase, EC 2.7.1.11) in muscle has been shown to be a regulatory enzyme for glycolysis, and, on the basis of the properties of this enzyme, a theory for metabolic control has been proposed

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Section: Resultsmentioning

confidence: 56%

mentioning

confidence: 99%

The activities of fructose 1,6-diphosphatase, phosphofructokinase and phosphoenolpyruvate carboxykinase in white muscle and red muscle

Opie¹,

Newsholme²

1967

Biochemical Journal

Self Cite

354

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“…Pyruvate dehydrogenase (PDH) and phosphofructokinase (PFK) activities were measured as described (11,12). ACC and CitLy activities were measured spectrophotometrically as reported previously (13,14).…”

Section: Fatty Acid and Glycogen Synthesis In Bat And Watmentioning

confidence: 99%

Cooperation between BAT and WAT of rats in thermogenesis in response to cold, and the mechanism of glycogen accumulation in BAT during reacclimation

Jakus

Sándor

Janáky

et al. 2008

Journal of Lipid Research

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Rats were exposed to cold and then reacclimated at neutral temperature. Changes related to fatty acid and glucose metabolism in brown and white adipose tissues (BAT and WAT) and in muscle were then examined. Of the many proteins involved in the metabolic response, two lipogenic enzymes, acetyl-coenzyme A carboxylase (ACC) and ATPcitrate lyase, were found to play a pervasive role and studied in detail. Expression of the total and phosphorylated forms of both lipogenic enzymes in response to cold increased in BAT but decreased in WAT. Importantly, in BAT, only the phosphorylation of the ACC1 isoenzyme was enhanced, whereas that of ACC2 remained unchanged. The activities of these enzymes and the in vivo rate of FFA synthesis together suggested that WAT supplies BAT with FFA and glucose by decreasing its own synthetic activity. Furthermore, cold increased the glucose uptake of BAT by stimulating the expression of components of the insulin signaling cascade, as observed by the enhanced expression and phosphorylation of Akt and GSK-3. In muscle, these changes were observed only during reacclimation, when serum insulin also increased. Such changes may be responsible for the extreme glycogen accumulation in the BAT of rats reacclimated from cold.-Jakus, P. B., A. Sandor, T. Janaky, and V. Farkas. Cooperation between BAT and WAT of rats in thermogenesis in response to cold, and the mechanism of glycogen accumulation in BAT during reacclimation. J. Lipid Res. 2008. 49: 332-339.

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“…The enzyme suspensions were centrifuged, the sedimented protein was dissolved in quartzdistilled water, and the solutions were treated with Sephadex G-25 (Pharmacia Fine Chemicals, Uppsala, Sweden). Activity determinations of hexosediphosphatase in crude extracts are complicated by the inhibitory effect of AMP [22,35,36]. I n order to remove AMP from the extracts, various methods were examined, e. g .…”

Section: Enzyme Activity Determinationsmentioning

confidence: 99%

Metabolic Differentiation of Distinct Muscle Types at the Level of Enzymatic Organization

Bass¹,

Brdiczka

Eyer

et al. 1969

European Journal of Biochemistry

624

245

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Activity levels of glycogen phosphorylase, hexokinase, triosephosphate dehydrogenase, lactate dehydrogenase, citrate synthase, 3-hydroxyacyl-CoA dehydrogenase, glycerolphosphate dehydrogenase (mitochondrial), and hexosediphosphatase have been determined in white (fast) muscles, red (slow) muscles, heart and smooth muscle of higher animals. The activities of these enzymes are taken as relative measures of metabolic capacities. Their ratios are interpreted as representing relations of different metabolic pathways or systems. I n all muscles investigated comparable ratios exist for phosphorylase/triosephosphate dehydrogenase (glycogenolysis/glycolysis), glycerolphosphate dehydrogenase/triosephosphate dehydrogenase (mitochondrial glycerolphosphate oxidation/glycolysis), triosephosphate dehydrogenase/lactate dehydrogenase (glycolysis/lactate fermentation), hexokinaselcitrate synthase (glucose phosphorylation/citric acid cycle) and 3-hydroxyacyl-CoA dehydrogenase/citrate synthase (fatty acid oxidation/citric acid cycle). With respect to the constancy of these ratios, consistent characteristics exist in the organization of the enzyme activity pattern. It is suggested that the more or less invariable coordination of these metabolic systems is not subject to metabolic differentiation. On the contrary, metabolic Werentiation is reflected by extreme variations of the following ratios : triosephosphate dehydrogenase/3-hydroxyacyl-CoA dehydrogenase (glycolysis/fatty acid oxidation), triosephosphate dehydrogenase/citrate synthase (glycolysis/citric acid cycle), lactate dehydrogenaselcitrate synthase (lactate fermentation/citric acid cycle), phosphorylase/hexokinase (glycogenolysis/glucose phosphorylation), and hexosediphosphatase/hexokinase (gluconeogenesis/ glucose phosphorylation). These variable enzyme activity ratios are discriminative magnitudes and make it possible to discern distinct metabolic types of muscle. White (fast) muscle is characterized by high capacities of glycogenolysis, glycolysis and lactate fermentation, whereas the capacities of glucose phosphorylation, citric acid cycle and fatty acid oxidation are low. Red (slow) muscles, heart and smooth muscle show inverse characteristics. I n white (fast) muscle, high activities of hexosediphosphatase and of mitochondrial glycerolphosphate dehydrogenase indicate that gluconeogenesis starting from glycerolphosphate or triosephosphate is probably important in this muscle type, and compensates for its low capacity of glucose phosphorylation.Enzymes. Adenylate deaminase, or AMP aminohydrolase (EC 3.5.4.6) ; adenylate kinase, or ATP: AMP phosphotransferase (EC 2.7.4.3) ; citrate synthase, or citrate oxaloacetate lyase (CoA-acetylating) (EC 4.1.3.7) ; glucosephosphate isomerase, or ~-glucose-B-phosphate ketol-isomerase (EC 5.3.1.9); glucose-6-phosphate dehydrogenase, or n-glucose-&phosphate: NADP oxidoreductase (EC 1.1.1.49); glycerolphosphate dehydrogenase, or ~-glycerol-3-phosphate: (acceptor) oxidoreductase (EC 1.1.99.5); 3-hydroxyacyl-CoA dehydrogenase, or L-3-hydro...

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The inhibition of skeletal-muscle fructose 1,6-diphosphatase by adenosine monophosphate

Cited by 52 publications

References 12 publications

The activities of fructose 1,6-diphosphatase, phosphofructokinase and phosphoenolpyruvate carboxykinase in white muscle and red muscle

The activities of fructose 1,6-diphosphatase, phosphofructokinase and phosphoenolpyruvate carboxykinase in white muscle and red muscle

Cooperation between BAT and WAT of rats in thermogenesis in response to cold, and the mechanism of glycogen accumulation in BAT during reacclimation

Metabolic Differentiation of Distinct Muscle Types at the Level of Enzymatic Organization

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