Inhibition of rat liver phosphofructokinase-2 by phosphoenolpyruvate and ADP |
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| Authors: | M Kretschmer E Hofmann |
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| Affiliation: | Institute of Physiological Chemistry, Karl-Marx-University, Leipzig, German Democratic Republic |
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| Abstract: | Phosphofructokinase-2 from rat liver is inhibited by phosphoenolpyruvate and ADP. Phosphoenolpyruvate reduces the maximum activity in respect to fructose-6-phosphate and ATP but does not give rise to complete inhibition of phosphofructokinase-2. ADP increases the apparent Michaelis constant of the enzyme for ATP and leaves the maximum activity in respect to ATP unchanged. The apparent Michaelis constant for fructose-6-phosphate is not influenced by ADP. |
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