Analyze enzyme kinetics using reciprocal substrate and velocity data. Estimate constants, inspect linear fit, and export neat results easily today.
| Substrate [S] | Velocity V | 1/[S] | 1/V |
|---|---|---|---|
| 0.5 | 0.83 | 2 | 1.204819 |
| 1 | 1.43 | 1 | 0.699301 |
| 1.5 | 1.88 | 0.666667 | 0.531915 |
| 2 | 2.22 | 0.5 | 0.45045 |
| 3 | 2.73 | 0.333333 | 0.3663 |
| 4 | 3.08 | 0.25 | 0.324675 |
| Substrate [S] | Velocity V | 1/[S] | 1/V |
|---|---|---|---|
| 0.5 | 0.83 | 2.000000 | 1.204819 |
| 1.0 | 1.43 | 1.000000 | 0.699301 |
| 1.5 | 1.88 | 0.666667 | 0.531915 |
| 2.0 | 2.22 | 0.500000 | 0.450450 |
| 3.0 | 2.73 | 0.333333 | 0.366300 |
| 4.0 | 3.08 | 0.250000 | 0.324675 |
The Lineweaver Burk form rewrites the Michaelis Menten equation into a straight line:
1 / V = (Km / Vmax)(1 / [S]) + 1 / Vmax
Here, y equals 1/V and x equals 1/[S]. The slope equals Km/Vmax. The y-intercept equals 1/Vmax. The x-intercept equals -1/Km. After linear regression, the calculator estimates Vmax, Km, slope, intercept, and R² from the reciprocal dataset.
This Lineweaver Burk plot calculator helps analyze enzyme kinetics using reciprocal data transformation. It accepts substrate concentration and velocity pairs, converts them into 1/[S] and 1/V values, then performs linear regression to estimate kinetic constants. The tool is useful for students, researchers, and laboratory teams who need a fast method for reviewing Michaelis Menten experiments.
The calculator reports slope, y-intercept, x-intercept, estimated Km, estimated Vmax, and coefficient of determination. These outputs help evaluate how well the transformed data follows a linear relationship. A stronger fit usually gives more confidence when reading kinetic trends from the reciprocal plot. Because the transformation amplifies low-value measurement error, the graph and R² should be reviewed carefully during interpretation.
The built-in plot displays reciprocal substrate values on the x-axis and reciprocal velocity values on the y-axis. A fitted line is drawn from the regression equation, making the relationship easier to inspect. This visual check helps identify unusual points, poor spacing, or patterns that suggest data quality issues. The data table below the result section also lists each reciprocal value for quick validation.
This page also includes export tools for convenient reporting. The CSV option downloads the calculated reciprocal table, while the PDF option creates a simple printable summary with key outputs. These features support homework submission, lab reporting, and record keeping. If you already have experimental pairs, you can paste them into the fields, calculate instantly, and review the plot without extra manual work.
It shows the linearized form of enzyme kinetics by plotting 1/V against 1/[S]. From the straight-line fit, you can estimate slope, y-intercept, x-intercept, Km, and Vmax.
Reciprocal transformation converts the Michaelis Menten curve into a straight line. That makes linear regression possible and helps derive kinetic constants from slope and intercept values.
The slope equals Km divided by Vmax. Once the line is fitted, the calculator uses that slope and the intercept to estimate both kinetic constants.
Vmax is calculated as the reciprocal of the y-intercept. Since the intercept equals 1/Vmax, taking its inverse gives the estimated maximum reaction velocity.
Km is found by multiplying the slope by Vmax. This follows directly from the straight-line form, where slope equals Km/Vmax.
The x-intercept equals negative one divided by Km. It provides another way to understand substrate affinity from the fitted line on the reciprocal graph.
R² indicates how well the fitted straight line matches the transformed data. A value closer to 1 suggests a stronger linear relationship in the reciprocal plot.
Yes. Lineweaver Burk plots can exaggerate error at low substrate concentrations because reciprocals magnify small measurement differences. Use the plot carefully and compare with other kinetic methods when needed.
Important Note: All the Calculators listed in this site are for educational purpose only and we do not guarentee the accuracy of results. Please do consult with other sources as well.