Is there anything left to say on enzyme kinetic constants and quasi-steady state approximation?
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Publication:431971
DOI10.1007/S10910-010-9770-7zbMATH Open1366.92055OpenAlexW2083017692MaRDI QIDQ431971FDOQ431971
Authors: Alberto Bersani, Guido Dell'Acqua 
Publication date: 3 July 2012
Published in: Journal of Mathematical Chemistry (Search for Journal in Brave)
Full work available at URL: https://doi.org/10.1007/s10910-010-9770-7
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Cites Work
- Michaelis-Menten kinetics at high enzyme concentrations
- Extending the quasi-steady state approximation by changing variables
- The Quasi-Steady-State Assumption: A Case Study in Perturbation
- Multiscale Modeling of Chemical Kinetics via the Master Equation
- Quasi steady-state approximations in complex intracellular signal transduction networks - a word of caution
- On the validity of the steady state assumption of enzyme kinetics
- The total quasi-steady-state approximation for complex enzyme reactions
- Introducing total substrates simplifies theoretical analysis at non-negligible enzyme concentrations: pseudo first-order kinetics and the loss of zero-order ultrasensitivity
- The total quasi-steady-state approximation for fully competitive enzyme reactions
- Properties of the Michaelis-Menten mechanism in phase space
- Quasi-steady state in the Michaelis-Menten system
Cited In (23)
- Quasi-steady-state laws in reversible model of enzyme kinetics
- Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations
- Enzyme kinetics: a critique of the quasi-steady-state approximation
- Extending the kinetic solution of the classic Michaelis--Menten model of enzyme action
- Enzyme kinetics for a two-step enzymic reaction with comparable initial enzyme-substrate ratios
- On the Hausdorff distance between the Heaviside step function and Verhulst logistic function
- Single-substrate enzyme kinetics: the quasi-steady-state approximation and beyond
- Uniform asymptotic expansions beyond the tQSSA for the Goldbeter-Koshland switch
- A novel approach to measure all rate constants in the simplest enzyme kinetics model
- On a stochastic approach to model the double phosphorylation/dephosphorylation cycle
- A comparative analysis of strict kinetic equations for the enzyme systems and equations obtained by the rapid equilibrium approach
- Characteristic, completion or matching timescales? An analysis of temporary boundaries in enzyme kinetics
- General mathematical formula for near equilibrium relaxation kinetics of basic enzyme reactions and its applications to find conformational selection steps
- A further step in the kinetic characterisation of the tyrosinase enzymatic system
- New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paper
- Simply conceiving the arrhenius law and absolute kinetic constants using the geometric distribution
- Metabolic rate constants: some computational aspects
- Analysis of the fractional modification of the monocyclic enzyme cascades, defined in an alternative way involving the two forms of the modified protein
- On the qualitative behaviour of oscillating biochemical systems: the stochastic approach
- A new mathematical formula to link near equilibrium relaxation kinetics and conformational selection steps in enzymatic reactions
- Functional adaptation of bone mechanical properties using a diffusive stimulus originated by dynamic loads in bone remodelling
- Interpretation of \(V/K\) isotope effects for enzymatic reactions exhibiting multiple isotopically sensitive steps
- The unreasonable effectiveness of the total quasi-steady state approximation, and its limitations
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