The total quasi-steady-state approximation for complex enzyme reactions

DOI10.1016/j.matcom.2008.02.009zbMath1157.92019OpenAlexW2006139156MaRDI QIDQ1010015

Enrico Bersani, Morten Gram Pedersen, Giuliana Cortese, Alberto Maria Bersani

Publication date: 3 April 2009

Published in: Mathematics and Computers in Simulation (Search for Journal in Brave)

Full work available at URL: https://doi.org/10.1016/j.matcom.2008.02.009

zbMATH Keywords

enzyme kineticsreverse engineeringsignal transduction

Mathematics Subject Classification ID

Dynamical systems in biology (37N25) Nonlinear ordinary differential equations and systems (34A34) Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45) Biochemistry, molecular biology (92C40)

Related Items (23)

New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paper ⋮ On the validity and errors of the pseudo-first-order kinetics in ligand-receptor binding ⋮ Application of optimal control techniques and advanced computing to the study of enzyme kinetics ⋮ Algorithmic criteria for the validity of quasi-steady state and partial equilibrium models: the Michaelis-Menten reaction mechanism ⋮ Uniform Asymptotic Expansions beyond the tQSSA for the Goldbeter--Koshland Switch ⋮ The quasi-steady-state approximations revisited: timescales, small parameters, singularities, and normal forms in enzyme kinetics ⋮ Michaelis-Menten equation for degradation of insoluble substrate ⋮ Is there anything left to say on enzyme kinetic constants and quasi-steady state approximation? ⋮ Mathematical Modelling of Metapopulation Dynamics: Revisiting its Meaning ⋮ Partial equilibrium approximations in apoptosis. I: The intracellular-signaling subsystem ⋮ Deterministic and stochastic models of enzymatic networks-applications to pharmaceutical research ⋮ Metabolic rate constants: some computational aspects ⋮ On a stochastic approach to model the double phosphorylation/dephosphorylation cycle ⋮ Reduced models of networks of coupled enzymatic reactions ⋮ Modeling the action of drugs on cellular enzymes by means of optimal control techniques ⋮ A perturbation solution of Michaelis-Menten kinetics in a ``total framework ⋮ A study case for the analysis of asymptotic expansions beyond the tQSSA for inhibitory mechanisms in enzyme kinetics. ⋮ Leading order asymptotics in the Goldbeter-Koshland switch ⋮ Single-substrate enzyme kinetics: the quasi-steady-state approximation and beyond ⋮ The total quasi-steady-state approximation for complex enzyme reactions ⋮ A new Michaelis-Menten equation valid everywhere multi-scale dynamics prevails ⋮ Introducing total substrates simplifies theoretical analysis at non-negligible enzyme concentrations: pseudo first-order kinetics and the loss of zero-order ultrasensitivity ⋮ Singular Perturbation Techniques and Asymptotic Expansions for Some Complex Enzyme Reactions

Cites Work

• Unnamed Item
• Michaelis-Menten kinetics at high enzyme concentrations
• Quasi steady-state approximations in complex intracellular signal transduction networks - a word of caution
• Time-dependent closed form solutions for fully competitive enzyme reactions
• The total quasi-steady-state approximation for complex enzyme reactions
• On the validity of the steady state assumption of enzyme kinetics
• Extending the quasi-steady state approximation by changing variables
• The total quasi-steady-state approximation is valid for reversible enzyme kinetics
• The Quasi-Steady-State Assumption: A Case Study in Perturbation

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