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

DOI10.1007/S10910-008-9460-XMaRDI QIDQ1028043zbMATH OpenOpenAlexFDO

Authors Bo Li, Yuefeng Shen, Bang-He 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)

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Cites work

• scientific article; zbMATH DE number 3835792 (Why is no real title available?)
• scientific article; zbMATH DE number 3135277 (Why is no real title available?)
• scientific article; zbMATH DE number 3484411 (Why is no real title available?)
• Dynamical models in biology
• Enzyme kinetics of multiple alternative substrates
• Simple mathematical models with very complicated dynamics
• The Quasi-Steady-State Assumption: A Case Study in Perturbation

Cited in

(8)

• 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
• Estimation of rate constants in nonlinear reactions involving chemical inactivation of oxidation catalysts
• Determination of kinetic parameters of enzyme-catalyzed reactions with a minimum number of velocity measurements
• A much better replacement of the Michaelis-Menten equation and its application
• Metabolic rate constants: some computational aspects

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