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- W2082654152 abstract "Abstract Yeast phosphofructokinase (ATP: d -fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) desensitized to ATP inhibition by the method of Afting et al. ((1971) Arch. Biochem. Biophys. 143, 587) exhibits normal Michaelis kinetics as judged by a double reciprocal plot or by a Hill plot with an apparent Km of 0.095 mM for fructose 6-phosphate which is about three times less than the minimum value observed for the untreated enzyme. The desensitized phosphofructokinase is neither inhibited to any great extent by citrate, nor activated by AMP. However, the desensitized phosphofructokinase is still activated by NH4+. The desensitized phosphofructokinase can be reconverted to the ATP-sensitive phosphofructokinase by preincubating the enzyme at 28 °C with 3 mM ATP, 10 mM citrate, or both at pH 6.8 or 7.5. These results may be interpreted in terms of the model for allosteric enzymes proposed by Monod et al. ((1965) J. Mol. Biol. 12, 88) where ATP-sensitive phosphofructokinase which predominates in the absence of ligands is converted to the desensitized phosphofructokinase form in a synergistic manner by preincubation of the enzyme with the positive effectors and salts of fluoride and magnesium." @default.
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- W2082654152 date "1972-09-01" @default.
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- W2082654152 title "Some kinetic properties of yeast phosphofructokinase desensitized to inhibition by adenosine triphosphate" @default.
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- W2082654152 doi "https://doi.org/10.1016/0005-2744(72)90050-2" @default.
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