Enzyme Kinetics Basics

The Michaelis-Menten equation describes the initial reaction velocity as a function of substrate concentration. It is significant in enzyme kinetics as it provides insights into the behavior of enzymes and their substrates, allowing for the determination of key parameters such as Vmax and KM.

KM is the substrate concentration that yields half of the maximum reaction velocity (½ Vmax). It is a measure of the affinity of the enzyme for its substrate, providing valuable information about the enzyme-substrate interaction.

The Lineweaver-Burk equation is derived by taking the reciprocal of both sides of the Michaelis-Menten equation. This manipulation results in a linear equation that can be used to determine Vmax and KM.

<p>In the Eadie-Scatchard plot, multiplication with (KM + [S]) is performed to linearize the Michaelis-Menten equation. This manipulation transforms the equation into a linear form, facilitating the determination of Vmax and KM.</p> Signup and view all the answers

<p>The Hanes-Woolf plot is used to linearize the Michaelis-Menten equation by plotting v/[S] against v. This linearization process simplifies the determination of Vmax and KM, providing valuable insights into the enzyme-substrate interaction.</p> Signup and view all the answers