Enzyme kinetics at high enzyme concentration
From MaRDI portal
Publication:886790
DOI10.1006/bulm.1999.0163zbMath1323.92099OpenAlexW2095889937WikidataQ52078698 ScholiaQ52078698MaRDI QIDQ886790
Santiago Schnell, Philip K. Maini
Publication date: 27 October 2015
Published in: Bulletin of Mathematical Biology (Search for Journal in Brave)
Full work available at URL: https://doi.org/10.1006/bulm.1999.0163
Related Items (53)
Susceptibilities of an irreversible Michaelis-Menten enzyme ⋮ New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paper ⋮ The total quasi-steady-state for multiple alternative substrate reactions ⋮ Stochastic enzyme kinetics and the quasi-steady-state reductions: application of the slow scale linear noise approximation à la Fenichel ⋮ Heineken, 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 binding ⋮ Approaches for the estimation of timescales in nonlinear dynamical systems: timescale separation in enzyme kinetics as a case study ⋮ Extension and justification of quasi-steady-state approximation for reversible bimolecular binding ⋮ Quasi-steady-state approximations derived from the stochastic model of enzyme kinetics ⋮ A new piecewise spectral homotopy analysisof the Michaelis-Menten enzymatic reactions model ⋮ Natural parameter conditions for singular perturbations of chemical and biochemical reaction networks ⋮ The total quasi-steady-state approximation is valid for reversible enzyme kinetics ⋮ Analysis of compartmental models of ligand-induced endocytosis ⋮ Perturbation theory in the catalytic rate constant of the Henri-Michaelis-Menten enzymatic reaction ⋮ Substrate and enzyme concentration dependence of the Henri-Michaelis-Menten model probed by numerical simulation ⋮ Algorithmic criteria for the validity of quasi-steady state and partial equilibrium models: the Michaelis-Menten reaction mechanism ⋮ The total quasi-steady-state approximation for fully competitive enzyme reactions ⋮ The quasi-steady-state approximations revisited: timescales, small parameters, singularities, and normal forms in enzyme kinetics ⋮ On approximate analytical solutions of differential equations in enzyme kinetics using homotopy perturbation method ⋮ An improved method to measure all rate constants in the simplest enzyme kinetics model ⋮ Trend to equilibrium for a reaction-diffusion system modelling reversible enzyme reaction ⋮ Theory on the rate equation of Michaelis-Menten type single-substrate enzyme catalyzed reactions ⋮ Partial equilibrium approximations in apoptosis. I: The intracellular-signaling subsystem ⋮ Quasi-steady-state kinetics at enzyme and substrate concentrations in excess of the Michaelis-Menten constant ⋮ All the trinomial roots, their powers and logarithms from the Lambert series, Bell polynomials and Fox-Wright function: illustration for genome multiplicity in survival of irradiated cells ⋮ Computing quasi-steady state reductions ⋮ A simplified perturbation solution of Michaelis-Menten kinetics equations in a ``total framework ⋮ Applying structural transition theory to describe enzyme kinetics in heterogeneous systems ⋮ Competitive effects in bacterial mRNA decay ⋮ Metabolic rate constants: some computational aspects ⋮ Analysis of the dynamical behavior for enzyme-catalyzed reactions with impulsive input ⋮ Nonstandard finite difference schemes for Michaelis–Menten type reaction‐diffusion equations ⋮ Quasi-steady state in the Michaelis-Menten system ⋮ From enzyme kinetics to epidemiological models with Michaelis-Menten contact rate: design of nonstandard finite difference schemes ⋮ Theoretical and computational studies of some bioreactor models ⋮ Reduced models of networks of coupled enzymatic reactions ⋮ Stochastic approaches for modelling in vivo reactions ⋮ Repair of irradiated cells by Michaelis-Menten enzyme catalysis: the Lambert function for integrated rate equations in description of surviving fractions ⋮ Mathematical modeling for the prevention of methanol poisoning through ethanol by impulsive way ⋮ A perturbation solution of Michaelis-Menten kinetics in a ``total framework ⋮ Why substrate depletion has apparent first-order kinetics in enzymatic digestion ⋮ Single-substrate enzyme kinetics: the quasi-steady-state approximation and beyond ⋮ Irreversible linear pathways in enzymatic reactions: analytical solution using the homotopy perturbation method ⋮ Asymptotic expansions in enzyme reactions with high enzyme concentrations ⋮ Efficacy of quasi-steady-state approximation in Michaelis-Menten kinetics: a stochastic signature ⋮ Sufficient Conditions for Coordination of Coupled Nonlinear Biochemical Systems: Analysis of a Simple, Representative Example ⋮ Maini's many contributions to mathematical enzyme kinetics: a review ⋮ 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 new Michaelis-Menten equation valid everywhere multi-scale dynamics prevails ⋮ Hunting $\varepsilon$: The Origin and Validity of Quasi-Steady-State Reductions in Enzyme Kinetics ⋮ Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations ⋮ Effects of periodic input on the quasi-steady state assumptions for enzyme-catalysed reactions
This page was built for publication: Enzyme kinetics at high enzyme concentration