Michaelis-Menten equation for degradation of insoluble substrate

DOI10.1016/j.mbs.2017.11.011zbMath1380.92025OpenAlexW2775611909WikidataQ47590161 ScholiaQ47590161MaRDI QIDQ1698530

Jeppe Kari, Kim Borch, Peter Westh, Morten Andersen

Publication date: 15 February 2018

Published in: Mathematical Biosciences (Search for Journal in Brave)

Full work available at URL: https://rucforsk.ruc.dk/ws/files/60582123/MM_substrate_conservation.pdf

zbMATH Keywords

parameter estimationenzyme kineticsMichaelis-Menten

Mathematics Subject Classification ID

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

Cites Work

• Michaelis-Menten kinetics at high enzyme concentrations
• A perturbation solution of Michaelis-Menten kinetics in a ``total framework
• The total quasi-steady-state approximation for complex enzyme reactions
• On the validity of the steady state assumption of enzyme kinetics
• Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations
• Extending the quasi-steady state approximation by changing variables
• Reduced models of networks of coupled enzymatic reactions
• 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
• The total quasi-steady-state approximation for fully competitive enzyme reactions
• Properties of the Michaelis-Menten mechanism in phase space
• Single-substrate enzyme kinetics: the quasi-steady-state approximation and beyond
• New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paper
• The Quasi-Steady-State Assumption: A Case Study in Perturbation

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