The Lineweaver-Burk plot, also known as the double-reciprocal plot, is a graphical representation used to determine important kinetic parameters of an enzyme-catalyzed reaction, specifically the Michaelis constant (𝐾𝑚) and the maximum reaction velocity (𝑉max).
Lineweaver-Burk Equation
![Lineweaver-Burk Equation](https://static.wixstatic.com/media/bd93cb_619f1c5726cd42eeaef63a8e66dc2223~mv2.png/v1/fill/w_165,h_52,al_c,q_85,enc_avif,quality_auto/bd93cb_619f1c5726cd42eeaef63a8e66dc2223~mv2.png)
Description
The Lineweaver-Burk plot, or the double reciprocal plot, graphs 1/v (reciprocal of the reaction rate) against 1/[S] (reciprocal of the substrate concentration).
This transformation facilitates a linear relationship that simplifies the determination of Vmax and Km.
![Enzyme Kinetics (Lineweaver-Burk Plot)](https://static.wixstatic.com/media/bd93cb_1b18beaafb244694879a4f8c6f1a854e~mv2.png/v1/fill/w_980,h_669,al_c,q_90,usm_0.66_1.00_0.01,enc_avif,quality_auto/bd93cb_1b18beaafb244694879a4f8c6f1a854e~mv2.png)
In this plot:
The y-intercept equals 1/Vmax.
The x-intercept is −1/−Km.
The slope represents Vmax/Km.
Advantages and Uses
The linear nature of the Lineweaver-Burk plot allows for a straightforward extraction of kinetic parameters. Additionally, this plot is particularly valuable in enzyme inhibition studies.
By comparing changes in the plot's slope, y-intercept, and x-intercept, one can deduce the type of inhibition (competitive, non-competitive, or uncompetitive) affecting the enzyme.