Quasi-steady-state kinetics at enzyme and substrate concentrations in excess of the Michaelis-Menten constant
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Publication:2210002
DOI10.1016/J.JTBI.2006.12.005zbMATH Open1451.92159OpenAlexW2038536277WikidataQ51925032 ScholiaQ51925032MaRDI QIDQ2210002FDOQ2210002
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
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Cites Work
- An Algorithm for Least-Squares Estimation of Nonlinear Parameters
- Michaelis-Menten kinetics at high enzyme concentrations
- Enzyme kinetics at high enzyme concentration
- Extending the quasi-steady state approximation by changing variables
- Stochastic approaches for modelling in vivo reactions
- On the validity of the steady state assumption of enzyme kinetics
- 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
- Uniform asymptotic expansions beyond the tQSSA for the Goldbeter-Koshland switch
- 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
- 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
- Title not available (Why is that?)
- 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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