Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations
Analytic approximations of the time-evolution of the single enzyme-substrate reaction are valid for all but a small region of parameter space in the positive initial enzyme-initial substrate concentration plane. We find velocity equations for the substrate decomposition and product formation with the aid of the total quasi-steady-state approximation and an aggregation technique for cases where neither the more normally employed standard nor reverse quasi-steady-state approximations are valid. Applications to determining reaction kinetic parameters are discussed. (C) 2001 Elsevier Science Ltd. All rights reserved.
total quasi-steady-state approximation aggregation technique fitting procedure singular perturbation