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- W2005462785 abstract "1. Phosphofructokinase purified from flounder liver is characterized by sigmoidal kinetics with fructose 6-phosphate as substrate. 2. The enzyme is inhibited at higher ATP levels at both pH 6.9 and 8.2. he inhibition is more pronounced at pH 6.9. 3. This inhibition can be relieved by inorganic phosphate, fructose 6-phosphate, AMP and cyclic AMP. 4. In lower concentrations ADP acts as a deinhibitor, but in higher concentrations the effect is vanishing. 5. Citrate and phosphoenolpyruvate are inhibitors. 6. Fructose-1,6-diphosphate and creatinphosphate are without effect. 7. With increasing Mg2+ level hyperbolic response curves are found with low ATP concentrations. With high ATP levels biphasic curves are demonstrated. 8. The enzyme behaves like mammalian phosphofructokinases but show some quantitative and qualitative differences." @default.
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- W2005462785 date "1981-01-01" @default.
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- W2005462785 title "Kinetic properties of phosphofructokinase from the flounder (Platichtys flesus L.)" @default.
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- W2005462785 doi "https://doi.org/10.1016/0305-0491(81)90333-3" @default.
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