Characteristic, completion or matching timescales? An analysis of temporary boundaries in enzyme kinetics.

ABSTRACT: Scaling analysis exploiting timescale separation has been one of the most important techniques in the quantitative analysis of nonlinear dynamical systems in mathematical and theoretical biology. In the case of enzyme catalyzed reactions, it is often overlooked that the characteristic timescales used for the scaling the rate equations are not ideal for determining when concentrations and reaction rates reach their maximum values. In this work, we first illustrate this point by considering the classic example of the single-enzyme, single-substrate Michaelis-Menten reaction mechanism. We then extend this analysis to a more complicated reaction mechanism, the auxiliary enzyme reaction, in which a substrate is converted to product in two sequential enzyme-catalyzed reactions. In this case, dep

SUBMITTER: Eilertsen J 

PROVIDER: S-EPMC6612542 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature