A kinetic analysis of coupled (or auxiliary) enzyme reactions

DOI10.1007/S11538-018-0513-4MaRDI QIDQ1633265zbMATH OpenOpenAlexWikidataFDO

Authors 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

zbMATH Keywords

auxiliary enzyme assaycoupled enzyme reactionsinitial rate experimentsreactant-stationary approximationSchnell-Mendoza equationsingular perturbation analysisslow manifoldtimescale separation

Mathematics Subject Classification ID

Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45)

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Cites work

• 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
• Michaelis-Menten kinetics at high enzyme concentrations
• Multiple time scale dynamics
• On the validity and errors of the pseudo-first-order kinetics in ligand-receptor binding
• On the validity of the steady state assumption of enzyme kinetics
• Quasi steady state and partial equilibrium approximations: their relation and their validity
• Quasi-steady-state approximation in the mathematical modeling of biochemical reaction networks
• Simplification and Scaling
• The Quasi-Steady-State Assumption: A Case Study in Perturbation

Cited in

(13)

• Determination of kinetic parameters of enzyme-catalyzed reactions with a minimum number of velocity measurements
• Using singular perturbation theory to determine kinetic parameters in a non-standard coupled enzyme assay
• Kinetic behaviour of proenzymes activation in the presence of different inhibitors for both activating and activated enzymes
• On a stochastic approach to model the double phosphorylation/dephosphorylation cycle
• Characteristic, completion or matching timescales? An analysis of temporary boundaries in enzyme kinetics
• A study of the temperature dependence of bienzyme systems and enzymatic chains
• Analysis of Kinetic Reaction Mechanisms
• Analysis of the Michaelis-Menten mechanism in an immobilised enzyme reactor
• scientific article; zbMATH DE number 903883 (Why is no real title available?)
• Singular perturbation techniques and asymptotic expansions for some complex enzyme reactions
• The effectiveness of synergistic enzymatic reaction with limited mediator stability
• Natural parameter conditions for singular perturbations of chemical and biochemical reaction networks
• Phase-plane geometries in coupled enzyme assays

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