The observed kinetics of reactions catalyzed by immobilized enzymes in microreactors may differ from their kinetics in well-mixed solution-phase reactors. While the steady-state differences have been analyzed before, the time-dependent differences have not been explored. In the present study, therefore, an initial feasibility analysis has been conducted to identify permissible regions for the kinetic parameters for dynamics solutions to exist. For a reaction catalyzed by alkaline phosphatase, it has been shown that the choices of the values of three vital parameters are inter-related and restricted to certain nonlinear loci. These limits add to the limits imposed by thermodynamic requirements, and they are important in determining dynamic behavior.