A kinetic analysis of coupled (or auxiliary) enzyme reactions
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Publication:1633265
DOI10.1007/s11538-018-0513-4zbMath1404.92083OpenAlexW2894836979WikidataQ57025169 ScholiaQ57025169MaRDI QIDQ1633265
Santiago Schnell, Justin S. Eilertsen
Publication date: 19 December 2018
Published in: Bulletin of Mathematical Biology (Search for Journal in Brave)
Full work available at URL: https://doi.org/10.1007/s11538-018-0513-4
singular perturbation analysisslow manifoldtimescale separationauxiliary enzyme assaycoupled enzyme reactionsinitial rate experimentsreactant-stationary approximationSchnell-Mendoza equation
Related Items (6)
Natural parameter conditions for singular perturbations of chemical and biochemical reaction networks ⋮ Using singular perturbation theory to determine kinetic parameters in a non-standard coupled enzyme assay ⋮ Phase-plane geometries in coupled enzyme assays ⋮ On a stochastic approach to model the double phosphorylation/dephosphorylation cycle ⋮ Characteristic, completion or matching timescales? An analysis of temporary boundaries in enzyme kinetics ⋮ Singular Perturbation Techniques and Asymptotic Expansions for Some Complex Enzyme Reactions
Cites Work
- Michaelis-Menten kinetics at high enzyme concentrations
- Multiple time scale dynamics
- Quasi-steady-state approximation in the mathematical modeling of biochemical reaction networks
- On the validity of the steady state assumption of enzyme kinetics
- Classical quasi-steady state reduction -- a mathematical characterization
- Extending the quasi-steady state approximation by changing variables
- Introducing total substrates simplifies theoretical analysis at non-negligible enzyme concentrations: pseudo first-order kinetics and the loss of zero-order ultrasensitivity
- On the validity and errors of the pseudo-first-order kinetics in ligand-receptor binding
- The Quasi-Steady-State Assumption: A Case Study in Perturbation
- Quasi steady state and partial equilibrium approximations: their relation and their validity
- Simplification and Scaling
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