Enter your Km (Michaelis Constant), Vmax (Maximum Reaction Velocity), and Substrate Concentrations to generate a Lineweaver-Burk Plot and calculate the Y-Intercept (1/Vmax), X-Intercept (-1/Km), Slope (Km/Vmax), and R² Correlation Coefficient — giving you a full double-reciprocal breakdown of your enzyme kinetics data.
Y-Intercept (1/Vmax)
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X-Intercept (-1/Km)
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Slope (Km/Vmax)
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R² (Correlation Coefficient)
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The Lineweaver-Burk plot is used in enzyme kinetics to determine Km and Vmax values from experimental data. It transforms the hyperbolic Michaelis-Menten equation into a linear relationship by plotting 1/v against 1/[S].
The y-intercept equals 1/Vmax, the x-intercept equals -1/Km, and the slope equals Km/Vmax. These values allow you to calculate the actual Km and Vmax parameters for your enzyme.
The main advantage is that it linearizes the Michaelis-Menten equation, making it easier to determine Km and Vmax values graphically. It also allows for easy identification of different types of enzyme inhibition.
The double reciprocal transformation amplifies errors in measurements, especially at low substrate concentrations. This can lead to inaccurate parameter estimates if the data contains experimental errors.
Use a range of substrate concentrations both below and above the Km value. Include at least 5-6 different concentrations spanning from 0.2×Km to 10×Km for the most accurate results.
The R² (correlation coefficient) indicates how well your data fits a linear relationship. Values closer to 1.0 indicate better linearity and more reliable Km and Vmax calculations.