Properties of the Michaelis-Menten mechanism in phase space
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Publication:2465865
Abstract: We study the two-dimensional reduction of the Michaelis-Menten reaction of enzyme kinetics. First, we prove the existence and uniqueness of a slow manifold between the horizontal and vertical isoclines. Second, we determine the concavity of all solutions in the first quadrant. Third, we establish the asymptotic behaviour of all solutions near the origin, which generally is not given by a Taylor series. Finally, we determine the asymptotic behaviour of the slow manifold at infinity.
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Cites work
- Applications of centre manifold theory
- Asymptotic analysis of two reduction methods for systems of chemical reactions
- Forced-convergence iterative schemes for the approximation of invariant manifolds
- scientific article; zbMATH DE number 1581767 (Why is no real title available?)
- scientific article; zbMATH DE number 49110 (Why is no real title available?)
- scientific article; zbMATH DE number 193260 (Why is no real title available?)
- scientific article; zbMATH DE number 3442447 (Why is no real title available?)
- scientific article; zbMATH DE number 3448490 (Why is no real title available?)
- Invariant manifold methods for metabolic model reduction
- Mathematical biology. Vol. 1: An introduction.
- Mathematical physiology
- On the simple Michaelis-Menten mechanism for chemical reactions
- Projecting to a Slow Manifold: Singularly Perturbed Systems and Legacy Codes
- Singular perturbation methods for ordinary differential equations
- The Quasi-Steady-State Assumption: A Case Study in Perturbation
Cited in
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- Heineken, Tsuchiya and Aris: ``On the mathematical status of the pseudo-steady state hypothesis. A classic from Volume 1 of \textit{Mathematical Biosciences}
- Properties of the lindemann mechanism in phase space
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- Is there anything left to say on enzyme kinetic constants and quasi-steady state approximation?
- Some mathematical properties of the Lindemann mechanism
- Reduction for Michaelis-Menten-Henri kinetics in the presence of diffusion
- Rigorous estimates for the quasi-steady state approximation of the Michaelis-Menten reaction mechanism at low enzyme concentrations
- Phase-plane geometries in coupled enzyme assays
- Accuracy versus predominance: reassessing the validity of the quasi-steady-state approximation
- The unique equilibrium's global exponential asymptotic stability of the irreversible Michaelis-Menten mechanism of enzyme kinetics
- Dynamics of the modified Michaelis--Menten system
- Extension and justification of quasi-steady-state approximation for reversible bimolecular binding
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