Michaelis-Menten kinetics at high enzyme concentrations

From MaRDI portal
Publication:253479

DOI10.1016/S0092-8240(03)00059-4zbMath1334.92185OpenAlexW2002162541WikidataQ79272810 ScholiaQ79272810MaRDI QIDQ253479

F. Blanchet-Sadri, M. Dambrine

Publication date: 8 March 2016

Published in: Bulletin of Mathematical Biology (Search for Journal in Brave)

Full work available at URL: https://doi.org/10.1016/s0092-8240(03)00059-4




Related Items (56)

New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paperA kinetic analysis of coupled (or auxiliary) enzyme reactionsThe total quasi-steady-state for multiple alternative substrate reactionsApproximation of enzyme kinetics for high enzyme concentration by a first order perturbation approachOn the anti-quasi-steady-state conditions of enzyme kineticsHeineken, Tsuchiya and Aris: ``On the mathematical status of the pseudo-steady state hypothesis. A classic from Volume 1 of \textit{Mathematical Biosciences}On the validity and errors of the pseudo-first-order kinetics in ligand-receptor bindingExtension and justification of quasi-steady-state approximation for reversible bimolecular bindingLayered decomposition for the model order reduction of timescale separated biochemical reaction networksQuasi-steady-state approximations derived from the stochastic model of enzyme kineticsA new piecewise spectral homotopy analysisof the Michaelis-Menten enzymatic reactions modelNatural parameter conditions for singular perturbations of chemical and biochemical reaction networksThe total quasi-steady-state approximation is valid for reversible enzyme kineticsAnalysis of compartmental models of ligand-induced endocytosisPerturbation theory in the catalytic rate constant of the Henri-Michaelis-Menten enzymatic reactionSubstrate and enzyme concentration dependence of the Henri-Michaelis-Menten model probed by numerical simulationKernel Ordinary Differential EquationsAlgorithmic criteria for the validity of quasi-steady state and partial equilibrium models: the Michaelis-Menten reaction mechanismThe unreasonable effectiveness of the total quasi-steady state approximation, and its limitationsThe total quasi-steady-state approximation for fully competitive enzyme reactionsThe quasi-steady-state approximations revisited: timescales, small parameters, singularities, and normal forms in enzyme kineticsMichaelis-Menten equation for degradation of insoluble substrateIs there anything left to say on enzyme kinetic constants and quasi-steady state approximation?Theory on the rate equation of Michaelis-Menten type single-substrate enzyme catalyzed reactionsPartial equilibrium approximations in apoptosis. I: The intracellular-signaling subsystemQuasi-steady-state kinetics at enzyme and substrate concentrations in excess of the Michaelis-Menten constantA transformed time-dependent Michaelis-Menten enzymatic reaction model and its asymptotic stabilityA simplified perturbation solution of Michaelis-Menten kinetics equations in a ``total frameworkApplying structural transition theory to describe enzyme kinetics in heterogeneous systemsCompetitive effects in bacterial mRNA decaySimplification of a complex signal transduction model using invariants and flow equivalent serversEnzyme kinetics with a twistDeterministic and stochastic models of enzymatic networks-applications to pharmaceutical researchLong-term behaviours of autocatalytic setsA collocation approach to solve the Riccati-type differential equation systemsSolution method for the transformed time-dependent Michaelis-Menten enzymatic reaction modelOperating regimes of covalent modification cycles at high enzyme concentrationsAn exponential matrix method for solving systems of linear differential equationsQuasi-steady state in the Michaelis-Menten systemOn a stochastic approach to model the double phosphorylation/dephosphorylation cycleDynamics of a system for migration from proliferative to dormant statusReduced models of networks of coupled enzymatic reactionsModeling the action of drugs on cellular enzymes by means of optimal control techniquesQuasi steady-state approximations in complex intracellular signal transduction networks - a word of cautionRepair of irradiated cells by Michaelis-Menten enzyme catalysis: the Lambert function for integrated rate equations in description of surviving fractionsA perturbation solution of Michaelis-Menten kinetics in a ``total frameworkGuaranteed error bounds for structured complexity reduction of biochemical networksSingle-substrate enzyme kinetics: the quasi-steady-state approximation and beyondThe total quasi-steady-state approximation for complex enzyme reactionsAsymptotic expansions in enzyme reactions with high enzyme concentrationsKrylov and steady-state techniques for the solution of the chemical master equation for the mitogen-activated protein kinase cascadeCharacteristic, completion or matching timescales? An analysis of temporary boundaries in enzyme kineticsGeneral mathematical formula for near equilibrium relaxation kinetics of basic enzyme reactions and its applications to find conformational selection stepsA new Michaelis-Menten equation valid everywhere multi-scale dynamics prevailsIntroducing total substrates simplifies theoretical analysis at non-negligible enzyme concentrations: pseudo first-order kinetics and the loss of zero-order ultrasensitivityHunting $\varepsilon$: The Origin and Validity of Quasi-Steady-State Reductions in Enzyme Kinetics




This page was built for publication: Michaelis-Menten kinetics at high enzyme concentrations