An improved method to measure all rate constants in the simplest enzyme kinetics model
From MaRDI portal
(Redirected from Publication:427459)
Recommendations
- A novel approach to measure all rate constants in the simplest enzyme kinetics model
- Metabolic rate constants: some computational aspects
- An alternative analysis of enzyme systems based on the whole reaction time: evaluation of the kinetic parameters and initial enzyme concentration
- Determination of kinetic parameters of enzyme-catalyzed reactions with a minimum number of velocity measurements
- Extending the kinetic solution of the classic Michaelis--Menten model of enzyme action
Cites work
- scientific article; zbMATH DE number 3135277 (Why is no real title available?)
- A novel approach to measure all rate constants in the simplest enzyme kinetics model
- Dynamical models in biology
- Enzyme kinetics at high enzyme concentration
- On the validity of the steady state assumption of enzyme kinetics
- The Quasi-Steady-State Assumption: A Case Study in Perturbation
Cited in
(7)- Determination of hammerhead ribozyme kinetic constants at high molar ratio ribozyme-substrate
- Single-substrate enzyme kinetics: the quasi-steady-state approximation and beyond
- A method for writing enzyme rate equations: Application to the estimation of the number and size of key proton families
- A novel approach to measure all rate constants in the simplest enzyme kinetics model
- 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
This page was built for publication: An improved method to measure all rate constants in the simplest enzyme kinetics model
Report a bug (only for logged in users!)Click here to report a bug for this page (MaRDI item Q427459)
