On the anti-quasi-steady-state conditions of enzyme kinetics

TL;DR

This paper identifies parameter regions where enzyme kinetics cannot be simplified using quasi-steady-state assumptions, providing necessary conditions and showing these regions are generally small, thus refining the understanding of enzyme reaction modeling.

Contribution

It introduces local necessary conditions for anti-quasi-steady-state in enzyme kinetics, complementing existing sufficient conditions and broadening the theoretical framework.

Findings

Explicit parameter regions where no quasi-steady-state reduction is applicable.

Demonstration that anti-quasi-steady-state regions are small.

Conditions for the accuracy of standard quasi-steady-state assumptions.

Abstract

Quasi-steady state reductions for the irreversible Michaelis--Menten reaction mechanism are of interest both from a theoretical and an experimental design perspective. A number of publications have been devoted to extending the parameter range where reduction is possible, via improved sufficient conditions. In the present note, we complement these results by exhibiting local conditions that preclude quasi-steady-state reductions (anti-quasi-steady-state), in the classical as well as in a broader sense. To this end, one needs to obtain necessary (as opposed to sufficient) conditions and determine parameter regions where these do not hold. In particular, we explicitly describe parameter regions where no quasi-steady-state reduction (in any sense) is applicable (anti-quasi-steady-state conditions), and we also show that -- in a well defined sense -- these parameter regions are small. From another perspective, we obtain local conditions for the accuracy of standard or total quasi-steady-state. Perhaps surprisingly, our conditions do not involve initial substrate.