Oscillations in the phosphofructokinase--fructose 1,6-bisphosphatase cycle. II. Influence of fructose 1,6-bisphosphatase on the character of oscillatory states.
Klaus Eschrich, Wolfgang Schellenberger, Eberhard Hofmann
Abstract
Klaus Eschrich, Wolfgang Schellenberger, Eberhard Hofmann
Abstract
The dynamic behaviour of an open futile cycle composed of phosphofructokinase and fructose 1,6-bisphosphatase has been investigated in a homogeneous reconstituted enzyme system in which the two enzymes cooperate with pyruvate kinase, adenylate kinase and glucose 6-phosphate isomerase. By the kinetic cooperation of phosphofructokinase and fructose 1,6-bisphosphatase various types of dynamic patterns can be generated. In the absence of fructose 1,6-bisphosphatase oscillations do not occur. As experimentally demonstrated, in a definite region of maximum activities of fructose 1,6-bisphosphatase sustained oscillations originate while at higher concentrations of the enzyme damped oscillations appear. At increasing concentrations of fructose 1,6-bisphosphatase damping is strengthened. Finally, at very high concentrations of fructose 1,6-bisphosphatase the metabolites relax monotonously to the stationary states. The observed oscillatory phenomena are mainly caused by the antagonistic effects of AMP on the kinetics of phosphofructokinase and fructose 1,6-bisphosphatase.
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The dynamic behaviour of an open futile cycle composed of phosphofructokinase and fructose 1,6-bisphosphatase has been investigated in a homogeneous reconstituted enzyme system in which the two enzymes cooperate with pyruvate kinase, adenylate kinase and glucose 6-phosphate isomerase. By the kinetic cooperation of phosphofructokinase and fructose 1,6-bisphosphatase various types of dynamic patterns can be generated. In the absence of fructose 1,6-bisphosphatase oscillations do not occur. As experimentally demonstrated, in a definite region of maximum activities of fructose 1,6-bisphosphatase sustained oscillations originate while at higher concentrations of the enzyme damped oscillations appear. At increasing concentrations of fructose 1,6-bisphosphatase damping is strengthened. Finally, at very high concentrations of fructose 1,6-bisphosphatase the metabolites relax monotonously to the stationary states. The observed oscillatory phenomena are mainly caused by the antagonistic effects of AMP on the kinetics of phosphofructokinase and fructose 1,6-bisphosphatase.
Key concepts: Phosphofructokinase, Fructose 1,6-bisphosphatase, Adenylate kinase, Fructose, Chemistry, Phosphofructokinase 2, Enzyme, Biochemistry