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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Cited in
(13)- scientific article; zbMATH DE number 3885699 (Why is no real title available?)
- Rigorous estimates for the quasi-steady state approximation of the Michaelis-Menten reaction mechanism at low enzyme concentrations
- On the anti-quasi-steady-state conditions of enzyme kinetics
- Is there anything left to say on enzyme kinetic constants and quasi-steady state approximation?
- Properties of the lindemann mechanism in phase space
- Reduction for Michaelis-Menten-Henri kinetics in the presence of diffusion
- Heineken, Tsuchiya and Aris: ``On the mathematical status of the pseudo-steady state hypothesis. A classic from Volume 1 of \textit{Mathematical Biosciences}
- Some mathematical properties of the Lindemann mechanism
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- Extension and justification of quasi-steady-state approximation for reversible bimolecular binding
- On the quasi-steady-state approximation in an open Michaelis-Menten reaction mechanism
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- Phase-plane geometries in coupled enzyme assays
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