Calculate and visualize Eadie-Hofstee plots for enzyme kinetics analysis with Km, Vmax, and substrate concentration data
Slope (-Km)
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Y-intercept (Vmax)
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Correlation Coefficient (R²)
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Data Points Analyzed
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The Eadie-Hofstee plot is a linear transformation of the Michaelis-Menten equation that plots velocity (v) against v/[S]. It provides an alternative method to determine Km and Vmax values, with the slope equal to -Km and the y-intercept equal to Vmax.
The slope of the Eadie-Hofstee plot equals -Km (negative Michaelis constant), while the y-intercept equals Vmax (maximum velocity). A steeper negative slope indicates lower substrate affinity (higher Km).
Eadie-Hofstee plots provide more even distribution of data points and are less sensitive to errors at low substrate concentrations compared to Lineweaver-Burk plots. They also give equal weighting to all data points.
Km represents the substrate concentration at which the reaction velocity is half of Vmax, indicating enzyme-substrate affinity. Vmax is the maximum reaction velocity when the enzyme is saturated with substrate.
A minimum of 5-6 data points spanning a wide range of substrate concentrations is recommended. Include concentrations both below and above the Km value for optimal accuracy.
The correlation coefficient indicates how well your data fits the linear model. Values closer to 1.0 indicate better linearity and more reliable Km and Vmax determinations.
Yes, Eadie-Hofstee plots are useful for analyzing enzyme inhibition. Different inhibition types produce characteristic changes in slope and intercept patterns compared to the uninhibited enzyme.