食品生物化学Chapter 18 Glycolysis.pptVIP

Regulation of Phosphofructokinase Phosphofructokinase is the “valve” [v?lv] 阀 controlling the rate of glycolysis. ATP is an allosteric inhibitor of this enzyme. In the presence of high ATP concentrations, phosphofructokinase behaves cooperatively, plots of enzyme activity versus fructose-6-phosphate are sigmoid, and the Km for fructose-6-phosphate is increased. Thus, when ATP levels are sufficiently high in the cytosol, glycolysis “turns off.” 磷酸果糖激酶 Under most cellular conditions, however, the ATP concentration does not vary over a large range. The ATP concentration in muscle during vigorous exercise, for example, is only about 10% lower than that during the resting state. The rate of glycolysis, however, varies much more. A large range of glycolytic rates cannot be directly accounted for by only a 10% change in ATP levels. How to achieve the regulation? AMP reverses the inhibition due to ATP Clearly, the activity of phosphofructokinase depends both on ATP and AMP levels and is a function of the cellular energy status. Phosphofructokinase activity is increased when the energy status falls and is decreased when the energy status is high. The rate of glycolysis activity thus decreases when ATP is plentiful and increases when more ATP is needed. AMP reverses the inhibition due to ATP, and AMP levels in cells can rise dramatically when ATP levels decrease, due to the action of the enzyme adenylate kinase腺苷酸激酶, which catalyzes the reaction. Adenylate kinase rapidly interconverts ADP, ATP, and AMP to maintain this equilibrium. Clearly, the activity of phosphofructokinase depends both on ATP and AMP levels and is a function of the cellular energy status. Phosphofructokinase activity is increased when the energy status falls and is decreased when the energy status is high. The rate of glycolysis activity thus decreases when ATP is plentiful and increases when more ATP is needed. Glycolysis and the citric acid cycle (Chapter 20) are coupled via phosp