A novel approach to measure all rate constants in the simplest enzyme kinetics model

DOI10.1007/S10910-008-9460-XzbMATH Open1182.92037OpenAlexW2008342533MaRDI QIDQ1028043FDOQ1028043

Bang-He Li, Yuefeng Shen, Bo Li

Publication date: 30 June 2009

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

Full work available at URL: https://doi.org/10.1007/s10910-008-9460-x

zbMATH Keywords

ordinary differential equationsMichaelis-Menten equationcatalytic constantMichaelis constant

Mathematics Subject Classification ID

Dynamical systems in biology (37N25) Computational methods for problems pertaining to biology (92-08) Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45)

Cites Work

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• Simple mathematical models with very complicated dynamics
• The Quasi-Steady-State Assumption: A Case Study in Perturbation
• Dynamical models in biology
• Enzyme kinetics of multiple alternative substrates

Cited In (6)

• A much better replacement of the Michaelis–Menten equation and its application
• Determination of hammerhead ribozyme kinetic constants at high molar ratio ribozyme-substrate
• An improved method to measure all rate constants in the simplest enzyme kinetics model
• A method for writing enzyme rate equations: Application to the estimation of the number and size of key proton families
• How to derive flux control coefficients from the rate equations of classical enzyme kinetics
• Determination of kinetic parameters of enzyme-catalyzed reactions with a minimum number of velocity measurements

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