Reduced models of networks of coupled enzymatic reactions

DOI10.1016/J.JTBI.2011.02.025zbMath1307.92107arXiv1101.1104OpenAlexW2090312078WikidataQ51595766 ScholiaQ51595766MaRDI QIDQ2263461

Ajit Kumar, Krešimir Josić

Publication date: 18 March 2015

Published in: Journal of Theoretical Biology (Search for Journal in Brave)

Full work available at URL: https://arxiv.org/abs/1101.1104

zbMATH Keywords

geometric singular perturbationMichaelis-Menten equationprotein interaction networkscoupled enzymatic networkstotal quasi-steady state

Mathematics Subject Classification ID

Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45) Biochemistry, molecular biology (92C40)

Related Items (14)

Tihonov theory and center manifolds for inhibitory mechanisms in enzyme kinetics ⋮ New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paper ⋮ Reciprocal enzyme regulation as a source of bistability in covalent modification cycles ⋮ A new piecewise spectral homotopy analysisof the Michaelis-Menten enzymatic reactions model ⋮ Classical quasi-steady state reduction -- a mathematical characterization ⋮ Using singular perturbation theory to determine kinetic parameters in a non-standard coupled enzyme assay ⋮ Uniform Asymptotic Expansions beyond the tQSSA for the Goldbeter--Koshland Switch ⋮ Michaelis-Menten equation for degradation of insoluble substrate ⋮ Piecewise linear and Boolean models of chemical reaction networks ⋮ A study case for the analysis of asymptotic expansions beyond the tQSSA for inhibitory mechanisms in enzyme kinetics. ⋮ Leading order asymptotics in the Goldbeter-Koshland switch ⋮ Perturbation and truncation of probability generating function methods for stiff chemical reactions ⋮ Introduction to the Geometric Theory of ODEs with Applications to Chemical Processes ⋮ Determining ``small parameters for quasi-steady state

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