In Michael is-Menten kinetics, using v (reaction rate) and [S] (substrate concen

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The Michaelis-Menten model (1) is the one of the simplest and best-known approaches to enzyme kinetics. It takes the form of an equation relating reaction velocity to substrate concentration for a system where a substrate S binds reversibly to an enzyme E to form an enzyme-substrate complex ES, which then reacts irreversibly to generate a product P and to regenerate the free enzyme E. This system can be represented schematically as follows: The Michaelis-Menten equation for this system is: E + S ==>> ES ==>> E + S Here, Vmax represents the maximum velocity achieved by the system, at maximum (saturating) substrate concentrations. KM (the Michaelis constant; sometimes represented as KS instead) is the substrate concentration at which the reaction velocity is 50% of the Vmax. [S] is the concentration of the substrate S. This is a plot of the Michaelis-Menten equation’s predicted reaction velocity as a function of substrate concentration, with the significance of the kinetic parameters Vmax and KM graphically depicted.

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