By Bernard L. Horecker, Earl R. Stadtman
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Additional info for Current topics in cellular regulation Vol. 5
The re sults suggest that caffeine (a purine analog) when included in the extrac tion fluid binds to the cyclic 3',5'-AMP sites on the enzyme, preventing the cyclic nucleotide or AMP from having accesses to these sites and thus preventing enzyme activation. This view is supported by the demon stration that the binding of cyclic 3',5'-AMP to pure phosphofructokinase is inhibited by caffeine (51). Furthermore, preincubation of the pure en zyme with cyclic 3',5'-AMP prevented inhibition by caffeine and by ATP 36 TAG E.
The question is still unresolved and is currently being investigated in our laboratory. VII. Physiological Interpretation of Phosphofructokinase Regulation A . Synchrony between Cellular Demand for High Energy and Enzyme Activity Variations in phosphofructokinase activity in connection with different physiological conditions have always been determined by changes in substrate levels in the cell. An increase in the levels of substrates beyond fructose-6-P in the glycolytic scheme suggests enzyme activation.
The mechanism of stimulation of fluke phosphofructokinase has been better understood in the light of more recent investigations by Stone and Mansour (120, 121). The enzyme which was isolated and partially puri fied from control parasites is almost completely inactive even when as sayed in the presence of concentrations of fructose-6-P as high as 10 mM and in the presence of different concentrations of ATP:Mg- + . There fore, the inactivity of the enzyme is not due to kinetic inhibition. 16 M of ammonium sulfate.
Current topics in cellular regulation Vol. 5 by Bernard L. Horecker, Earl R. Stadtman