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ADP-specific phosphofructokinase

The enzyme phosphofructokinase is allosteric, that is, it is made up of equivalent units that possess specific reaction sites for the fixation of the substrate and product. Each unit exists in two conformational states one active with more affinity for the substrate, and one inactive. The reaction products of phosphofructokinase (FDP and ADP) displace the conformational equilibrium in favor of the active form of the enzyme. This may create a destabilizing effect on the excess entropy production. In the glycolytic cycle, the allosteric properties of the phosphofructokinase may lead to oscillations. Consider the following simple model... [Pg.658]


See other pages where ADP-specific phosphofructokinase is mentioned: [Pg.223]    [Pg.223]    [Pg.224]    [Pg.225]    [Pg.334]    [Pg.223]    [Pg.223]    [Pg.224]    [Pg.225]    [Pg.334]    [Pg.191]    [Pg.345]    [Pg.351]    [Pg.518]    [Pg.263]    [Pg.296]    [Pg.586]    [Pg.378]   


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Phosphofructokinase

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