Diffusion fronts in enzyme-catalysed reactions

DOI10.1007/S10665-007-9142-XMaRDI QIDQ2458020zbMATH OpenOpenAlexFDO

Authors Graeme P. Boswell, Fordyce A. Davidson

Publication date 24 October 2007

Published in Journal of Engineering Mathematics (Search for Journal in Brave)

Full work available at URL https://doi.org/10.1007/s10665-007-9142-x

zbMATH Keywords

open systemquasi-steady statediffusible substrate

Mathematics Subject Classification ID

Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45)

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Cites work

• scientific article; zbMATH DE number 3991313 (Why is no real title available?)
• Effects of periodic input on the quasi-steady state assumptions for enzyme-catalysed reactions
• Handbook of linear partial differential equations for engineers and scientists
• On the quasi-steady-state assumption applied to Michaelis-Menten and suicide substrate reactions with diffusion
• On the spread of morphogens
• On the validity of the steady state assumption of enzyme kinetics
• Quasi-steady state assumptions for non-isolated enzyme-catalysed reactions
• The Quasi-Steady-State Assumption: A Case Study in Perturbation

Cited in

(12)

• Diffusion modifies the connectivity of kinetic schemes for multisite binding and catalysis
• Reduction for Michaelis-Menten-Henri kinetics in the presence of diffusion
• Rigorous derivation of Michaelis-Menten kinetics in the presence of slow diffusion
• On the quasi-steady-state assumption applied to Michaelis-Menten and suicide substrate reactions with diffusion
• scientific article; zbMATH DE number 5025588 (Why is no real title available?)
• Quasi-steady state assumptions for non-isolated enzyme-catalysed reactions
• Numerical solutions of strongly non-linear generalized Burgers-Fisher equation via meshfree spectral technique
• The application of enzyme reaction, nonlinear diffusion models to the malting process
• Monte Carlo simulations of enzymatic reactions in crowded media. Effect of the enzyme-obstacle relative size
• Michaelis-Menten equation for degradation of insoluble substrate
• Analysis of the dynamical behavior for enzyme-catalyzed reactions with impulsive input
• Noise slows the rate of Michaelis-Menten reactions

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