EadieHofsteePlot

The Eadie-Hofstee plot is a graphical method used in enzyme kinetics to analyze the relationship between reaction velocity and substrate concentration. It is derived from the Michaelis-Menten equation, which describes the rate of enzyme-catalyzed reactions. The Eadie-Hofstee plot specifically rearranges the Michaelis-Menten equation to plot velocity (v) on the y-axis against velocity divided by substrate concentration (v/[S]) on the x-axis. The resulting equation is linear, allowing for the determination of key kinetic parameters such as the maximum velocity (Vmax) and the Michaelis constant (Km). Vmax is represented by the y-intercept, and Km can be calculated from the slope and the y-intercept. While other graphical methods like the Lineweaver-Burk plot and Hanes-Woolf plot also exist for enzyme kinetic analysis, the Eadie-Hofstee plot is sometimes favored because it can be less prone to certain types of error, particularly when dealing with experimental data that may have higher variability at low substrate concentrations. The plot's linearity makes visual assessment of enzyme behavior and the identification of deviations from ideal Michaelis-Menten kinetics straightforward.