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

Cites Work

• Unnamed Item
• Michaelis-Menten kinetics at high enzyme concentrations
• Quasi steady-state approximations in complex intracellular signal transduction networks - a word of caution
• Enzyme kinetics for a two-step enzymic reaction with comparable initial enzyme-substrate ratios
• Enzyme kinetics at high enzyme concentration
• The total quasi-steady-state approximation for complex enzyme reactions
• Matrix differential calculus with applications to simple, Hadamard, and Kronecker products
• On the validity of the steady state assumption of enzyme kinetics
• Geometric singular perturbation theory for ordinary differential equations
• Normally hyperbolic invariant manifolds in dynamical systems
• Mathematical biology. Vol. 2: Spatial models and biomedical applications.
• The transition from differential equations to Boolean networks: A case study in simplifying a regulatory network model
• Analysis of the computational singular perturbation reduction method for chemical kinetics
• Extending the quasi-steady state approximation by changing variables
• The total quasi-steady-state approximation is valid for reversible enzyme kinetics
• Geometric singular perturbation theory in biological practice
• A multi-time-scale analysis of chemical reaction networks. I: Deterministic systems
• Quasi-steady state in the Michaelis-Menten system
• Mathematical model of the cell division cycle of fission yeast
• The Quasi-Steady-State Assumption: A Case Study in Perturbation
• On direct product matrices
• Some Theorems on Matrix Differentiation with Special Reference to Kronecker Matrix Products

This page was built for publication: Reduced models of networks of coupled enzymatic reactions