Quasi-steady-state kinetics at enzyme and substrate concentrations in excess of the Michaelis-Menten constant

DOI10.1016/J.JTBI.2006.12.005MaRDI QIDQ2210002zbMATH OpenOpenAlexWikidataFDO

Authors A. Rami Tzafriri, Elazer R. Edelman

Publication date 5 November 2020

Published in Journal of Theoretical Biology (Search for Journal in Brave)

Full work available at URL https://doi.org/10.1016/j.jtbi.2006.12.005

zbMATH Keywords

enzyme kineticsquasi-steady-state approximationMichaelis-Mentenrate equations

Mathematics Subject Classification ID

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

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Cites work

• An Algorithm for Least-Squares Estimation of Nonlinear Parameters
• Enzyme kinetics at high enzyme concentration
• Extending the quasi-steady state approximation by changing variables
• Michaelis-Menten kinetics at high enzyme concentrations
• On the validity of the steady state assumption of enzyme kinetics
• Stochastic approaches for modelling in vivo reactions
• The total quasi-steady-state approximation is valid for reversible enzyme kinetics

Cited in

(19)

• Michaelis-Menten kinetics at high enzyme concentrations
• Singular perturbation techniques and asymptotic expansions for some complex enzyme reactions
• Determination of hammerhead ribozyme kinetic constants at high molar ratio ribozyme-substrate
• Enzyme kinetics at high enzyme concentration
• Efficacy of quasi-steady-state approximation in Michaelis-Menten kinetics: a stochastic signature
• A study case for the analysis of asymptotic expansions beyond the tQSSA for inhibitory mechanisms in enzyme kinetics.
• Single-substrate enzyme kinetics: the quasi-steady-state approximation and beyond
• An approximate solution for the transient kinetic behavior of enzyme- catalyzed reactions: The irreversible Michaelis-Menten kinetics
• Zero-order ultrasensitivity: a study of criticality and fluctuations under the total quasi-steady state approximation in the linear noise regime
• The ``memory effect in a chain of biochemical reactions with a positive feedback is enhanced by substrate saturation described by Michaelis-Menten kinetics
• Uniform asymptotic expansions beyond the tQSSA for the Goldbeter-Koshland switch
• On the quasi-steady-state assumption applied to Michaelis-Menten and suicide substrate reactions with diffusion
• An alternative approach to Michaelis-Menten kinetics that is based on the renormalization group
• The total quasi-steady-state for multiple alternative substrate reactions
• scientific article; zbMATH DE number 2233481 (Why is no real title available?)
• Theory on the rate equation of Michaelis-Menten type single-substrate enzyme catalyzed reactions
• New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paper
• Introducing total substrates simplifies theoretical analysis at non-negligible enzyme concentrations: pseudo first-order kinetics and the loss of zero-order ultrasensitivity
• The quasi-steady-state approximations revisited: timescales, small parameters, singularities, and normal forms in enzyme kinetics

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