Allosteric oscillatory enzymes: influence of the number of protomers on metabolic periodicities.
The study of a concerted allosteric model for an enzyme activated by the reaction product shows that this system can generate sustained metabolic oscillations regardless of the number of protomers constituting the enzyme. The analysis extends the results previously obtained in a dimeric model for the phosphofructokinase reaction which produces glycolytic periodicities. When the substrate and product concentrations evolve on comparable time scales, the amplitude of oscillations significantly drops as the number of enzyme subunits evolves from 2 to 8. The width of the domain of substrate injection rates which produce oscillations and the periodic variation in enzyme activity also depend on the number of protomers and on the time scale structure of the system. Theoretical predictions are compared with the experiments on glycolytic oscillations in yeast and muscle, and with the structural characteristics of phosphofructokinase. The results are also discussed in relation with the mechanism of cyclic AMP oscillations in the slime mold Dictyostelium discoideum.
D000494:Allosteric Regulation; D000242:Cyclic AMP / Q000378:metabolism; D004023:Dictyostelium / Q000378:metabolism; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008954:Models, Biological; D010732:Phosphofructokinase-1 / Q000378:metabolism; D011485:Protein Binding
D004798:Enzymes; D000242:Cyclic AMP; D010732:Phosphofructokinase-1