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

DOI10.1016/J.MBS.2022.108870MaRDI QIDQ2164666zbMATH OpenOpenAlexFDO

Authors Justin S. Eilertsen, Santiago Schnell, S Walcher

Publication date 15 August 2022

Published in Mathematical Biosciences (Search for Journal in Brave)

Full work available at URL https://arxiv.org/abs/2112.04098

zbMATH Keywords

eigenvaluesMichaelis-Mentenquasi-steady-statesingular perturbationtimescales

Mathematics Subject Classification ID

Transformation and reduction of ordinary differential equations and systems, normal forms (34C20) Singular perturbations for ordinary differential equations (34E15) Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45)

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.

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Cited in

(15)

• On the quasi-steady-state approximation in an open Michaelis-Menten reaction mechanism
• The quasi-steady-state approximations revisited: timescales, small parameters, singularities, and normal forms in enzyme kinetics
• Two new regulatory properties arising from the transient phase kinetics of monocyclic enzyme cascades
• scientific article; zbMATH DE number 4053412 (Why is no real title available?)
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• A general solution for the steady-state kinetics of immobilized enzyme systems
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