Abstract
Taking as starting point a previous contribution about the kinetics of the transient phase and steady-state of monocyclic enzyme cascades, this paper suggest the definition and use of new regulatory modification properties involving the time elapses from the onset of the reaction to the attainment of the steady-state for a monocyclic enzyme cascade. A minimal set of simplifying assumptions allowing to derive analytical expressions for these properties has been used. From these general expressions we derive, as particular cases, other simpler expressions by using additional assumptions which have, therefore, a smaller range of validity. A discussion of the relationships between the kinetic parameters and concentrations needed to the additional assumption is observed is carried out. The goodness of our analysis has been tested by using numerical integration of the set of differential equation describing the kinetic behaviour of the cascade. The results obtained for a type of cascade are extrapolable to other different schemes of monocyclic enzyme cascades. Finally, a kinetic data analysis and an experimental design are suggested
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Varón, R., García-Moreno, M., García-Molina, F. et al. Two New Regulatory Properties Arising from the Transient Phase Kinetics of Monocyclic Enzyme Cascades. J Math Chem 38, 437–450 (2005). https://doi.org/10.1007/s10910-004-6895-6
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DOI: https://doi.org/10.1007/s10910-004-6895-6