ArticleBiophysical chemistry2018
A theory of reactant-stationary kinetics for a mechanism of zymogen activation.
Article in Biophysical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Using singular perturbation theory to determine kinetic parameters in a non-standard coupled enzyme assay.Journal of mathematical biology · 2020Article
- The quasi-steady-state approximations revisited: Timescales, small parameters, singularities, and normal forms in enzyme kinetics.Mathematical biosciences · 2020Article
- Characteristic, completion or matching timescales? An analysis of temporary boundaries in enzyme kinetics.Journal of theoretical biology · 2019Article
- Phase-plane geometries in coupled enzyme assays.Mathematical biosciences · 2018Article
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3 authors.
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Abstract
A theoretical analysis is performed on the nonlinear ordinary differential equations that govern the dynamics of a reaction mechanism of zymogen activation. The reaction consists of a primary non-observable zymogen activation reaction that it is coupled to an indicator (observable) reaction. The product of the first reaction is the enzyme of the indicator reaction, and both reactions are governed by the Michaelis-Menten reaction mechanism. Using singular perturbation methods, we derive asymptotic solutions that are valid under the quasi-steady-state and reactant-stationary assumptions. In particular, we obtain closed form solutions that are analogous to the Schnell-Mendoza equation for Michaelis-Menten type reactions. These closed-form solutions approximate the evolution of the observable reaction and provide the mathematical link necessary to measure the enzyme activity of the non-observable reaction. Conditions for the validity of the asymptotic solutions are also derived, and we demonstrate that these asymptotic expressions are applicable under reactant-stationary kinetics.
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