The Lineweaver-Burk plot, also known as a double reciprocal plot, is a graphical representation of the Lineweaver-Burk equation, derived from the Michaelis-Menten equation. This plot allows for the determination of key enzyme kinetic parameters, specifically the Michaelis constant (Km) and the maximum reaction rate (Vmax). These parameters provide insight into the affinity of an enzyme for its substrate and the maximal velocity achievable by the enzyme-catalyzed reaction, respectively. Graphically, the Lineweaver-Burk plot is a linear representation where the inverse of the reaction rate (1/v) is plotted against the inverse of the substrate concentration (1/[S]).
The usefulness of the Lineweaver-Burk plot lies in its ability to transform the hyperbolic relationship described by the Michaelis-Menten equation into a linear form. This linearization simplifies the process of determining Km and Vmax. Historically, this method was crucial for enzyme kinetics studies before the widespread availability of computer software capable of non-linear regression analysis. Although direct fitting of the Michaelis-Menten equation is now often preferred for its increased accuracy, the double reciprocal plot remains a valuable tool for visualizing enzyme kinetics data, estimating parameters, and quickly identifying deviations from Michaelis-Menten kinetics, such as those caused by enzyme inhibitors.
