Enzyme kinetics of multiple alternative substrates

DOI10.1023/A:1019139423811zbMath0993.92019OpenAlexW1594945568MaRDI QIDQ5928777

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Publication date: 3 April 2001

Published in: Journal of Mathematical Chemistry (Search for Journal in Brave)

Full work available at URL: https://doi.org/10.1023/a:1019139423811

Mathematics Subject Classification ID

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

Related Items (8)

The total quasi-steady-state for multiple alternative substrate reactions ⋮ Total least squares fitting Michaelis--Menten enzyme kinetic model function ⋮ A new piecewise spectral homotopy analysisof the Michaelis-Menten enzymatic reactions model ⋮ Analysis of compartmental models of ligand-induced endocytosis ⋮ The quasi-steady-state approximations revisited: timescales, small parameters, singularities, and normal forms in enzyme kinetics ⋮ A novel approach to measure all rate constants in the simplest enzyme kinetics model ⋮ A review of existence criteria for parameter estimation of the Michaelis-Menten regression model ⋮ Exact linear reduction for rational dynamical systems

Uses Software

• WAPR

Cites Work

• Unnamed Item
• Time-dependent closed form solutions for fully competitive enzyme reactions
• On the validity of the steady state assumption of enzyme kinetics
• On the Lambert \(w\) function
• Real values of the W -function
• Algorithm 743: WAPR--a Fortran routine for calculating real values of the W -function
• The Quasi-Steady-State Assumption: A Case Study in Perturbation

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