[Multiplicity of auto-oscillations and steady states in an open reaction catalyzed by E. coli phosphofructokinase. Quantitative model].
A quantitative mathematical model of two-substrate reaction catalized by phosphofructokinase from E. coli has been investigated. The model takes into account the tetrameric enzyme structure and resulting kinetic peculiarities of the reaction catalized, in particular, iso-and alosteric effects of ADP on enzyme activity. Fitting of the model parameters to experimental data allowed to approximate these data with good accuracy. The ranges of admitted rates of fructose-6-phosphate input and ATP regeneration at which autooscillations and multiple steady-states occur in the system have been calculated. A minimal open system with three enzymes has been proposed for experimental demonstration of the autooscillatory behaviour.
D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology*; D005635:Fructosediphosphates; D005636:Fructosephosphates; D008433:Mathematics; D008954:Models, Biological; D010732:Phosphofructokinase-1; D011487:Protein Conformation
D005635:Fructosediphosphates; D005636:Fructosephosphates; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1
Mnozhestvennost' stationarnykh sostoianiĭ i avtokolebaniia v otkrytoĭ reaktsii, kataliziruemoĭ fosfofruktokinazoĭ iz E. coli. Kolichestvennaia model'.