Open AccessPurification and Regulatory Properties of ATP‐Sensitive Phosphofructokinase from Yeast
Author(s) -
Atzpodien W.,
Bode H.
Publication year - 1970
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1970.tb00829.x
Subject(s) - phosphofructokinase , biochemistry , enzyme , yeast , phosphoenolpyruvate carboxykinase , inhibitory postsynaptic potential , effector , chemistry , enzyme assay , allosteric regulation , biology , glycolysis , neuroscience
Phosphofructokinase from baker's yeast has been purified 370‐fold. The purified enzyme is homogeneous as judged by analytical ultracentrifugation and disc electrophoresis. It exhibits the kinetic properties reported for phosphofructokinase from yeast and other sources. The purified enzyme is very sensitive to inhibition by ATP. The inhibition is pH‐dependent with a maximum around pH 7.5. The influence of different effectors on the enzymatic activity and on the inhibition by ATP are described. NH 4 + ions cause a general stimulation of enzymatic activity, while the sensitivity to ATP is abolished. ADP inhibits the enzyme at non‐inhibitory ATP levels and stimulates the activity at inhibitory concentrations of ATP. Phosphoenolpyruvate is a negative effector. Inorganic phosphate inhibits the activity by competition with Fru‐6‐ P and increases the inhibitory effect of ATP.