A transformed time-dependent Michaelis-Menten enzymatic reaction model and its asymptotic stability

DOI10.1007/s10910-013-0257-1zbMath1311.92072OpenAlexW1986858814MaRDI QIDQ2441094

Kristina Mallory, Robert A. van Gorder

Publication date: 21 March 2014

Published in: Journal of Mathematical Chemistry (Search for Journal in Brave)

Full work available at URL: https://doi.org/10.1007/s10910-013-0257-1

zbMATH Keywords

stabilitynonlinear dynamicsenzyme reactionsdynamic Michaelis-Menten model

Mathematics Subject Classification ID

Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45) Biochemistry, molecular biology (92C40)

Related Items (3)

An efficient Jacobi pseudospectral approximation for nonlinear complex generalized Zakharov system ⋮ Mathematical analysis of the heterogeneous photo-Fenton oxidation of acetic acid on structured catalysts ⋮ Solution method for the transformed time-dependent Michaelis-Menten enzymatic reaction model

Cites Work

• Michaelis-Menten kinetics at high enzyme concentrations
• A new piecewise spectral homotopy analysisof the Michaelis-Menten enzymatic reactions model
• Some issues on HPM and HAM methods: a convergence scheme
• Analytical solution of non-linear enzyme reaction equations arising in mathematical chemistry
• Comparison of homotopy analysis method and homotopy perturbation method through an evolution equation
• Enzyme kinetics for a two-step enzymic reaction with comparable initial enzyme-substrate ratios
• On approximate analytical solutions of differential equations in enzyme kinetics using homotopy perturbation method
• The total quasi-steady-state approximation is valid for reversible enzyme kinetics

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