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- W2000372697 abstract "Abstract The rate of conversion of Fru-6-P to Fru-1,6-P2 catalyzed by phosphofructokinase ATP: d -Fru -6-P 1-phosphotransferase, EC 2.7.1.11) is regulated by the inhibition of its activity by a high concentration of one of its substrates (ATP) and the relief of this inhibition by various effector metabolites. AMP specifically reverses the ATP inhibition of phosphofructokinase of yeast. In this communication, data re presented on the partial purification of yeast phosphofructokinase and its properties. The yeast phosphofructokinase prepared by the method described here was less sensitive to ATP inhibition than was the enzyme in the crude fraction. The enzyme, though stable at a concentration range of 8–10 mg protein per ml, lost half of its activity on dilution to about 0.8–1.0 mg protein per ml and on storing at 0°. The phosphofructokinase activity remaining after such dilution and storage appeared to be almost completely insensitive to ATP inhibition and AMP activation. This loss of phosphofructokinase activity and of its sensitivity to ATP inhibition as well as AMP activation could be prevented by diluting the enzyme and storing it in the presence of ATP, AMP or Fru-6-P but not in the presence of MgCl2 or NH4Cl." @default.
- W2000372697 created "2016-06-24" @default.
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- W2000372697 date "1970-05-01" @default.
- W2000372697 modified "2023-09-25" @default.
- W2000372697 title "Properties of yeast phosphofructokinase" @default.
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- W2000372697 doi "https://doi.org/10.1016/0005-2744(70)90110-5" @default.
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