Lineweaver–Burk Plot Generator

Figran

Fit Kₘ and Vₘₐₓ to your data, then draw the Michaelis–Menten plot and the Lineweaver–Burk plot.

  • Nonlinear Kₘ and Vₘₐₓ fit
  • Compare up to 6 conditions
  • Free SVG and 300 DPI PNG
Data
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TreatedA Michaelis–Menten0.00.51.01.50100200300[S] (ppm)v (counts/min²)KₘVₘₐₓB Lineweaver–Burk−200204060−0.010.000.010.020.031/[S] (ppm⁻¹)1/v (min²/count)1/Vₘₐₓ−1/KₘEnzyme kinetics plot

Results

ConditionnKₘ ± SE (ppm)Vₘₐₓ ± SE (counts/min²)R²Sy.xLB Kₘ / Vₘₐₓ
Treated120.06412 ± 0.00828195% CI: 0.04567 to 0.08257212.7 ± 6.94795% CI: 197.2 to 228.20.961310.930.04841 / 195.8

Michaelis–Menten and Lineweaver–Burk examples

Explore measured rates and illustrative comparisons, then load an example into the editor.

Puromycin-treated enzyme

The classic Puromycin treated-cell rates, fitted by nonlinear Michaelis–Menten regression.

Source: R datasets (Puromycin)

Treated vs untreated cells

Compare two conditions with repeated measurements.

Source: R datasets (Puromycin)

Illustrative

Wild type and two mutants

Compare three illustrative enzyme variants.

Eadie–Hofstee plot

Plot v against v/[S]; the slope is −Kₘ and the y-intercept is Vₘₐₓ.

Source: R datasets (Puromycin)

Hanes–Woolf plot

Plot [S]/v against [S]; the slope is 1/Vₘₐₓ and the x-intercept is −Kₘ.

Source: R datasets (Puromycin)

Illustrative

Lab report with replicates

Illustrative replicates include a zero substrate blank.

How to make an enzyme kinetics graph

Enter initial rates or parameters, choose a plot and download your figure.

  1. 1Enter your data

    Paste substrate concentrations and initial rates, or enter Kₘ and Vₘₐₓ.

  2. 2Choose the plot

    Check the fit and show the Michaelis–Menten plot, a transformed plot, or both.

  3. 3Download the result

    Save the figure or copy the results and figure legend.

How to read a Lineweaver–Burk plot

The double reciprocal plot turns the Michaelis–Menten equation into a line.

TreatedLineweaver–Burk−200204060−0.0050.0000.0050.0100.0150.0200.0251/[S] (ppm⁻¹)1/v (min²/count)1/Vₘₐₓ−1/Kₘ123

1/v = (Kₘ/Vₘₐₓ) × 1/[S] + 1/Vₘₐₓ

The original double-reciprocal method was described by Lineweaver and Burk (1934).

  1. The slope is Kₘ/Vₘₐₓ.
  2. The y-intercept is 1/Vₘₐₓ.
  3. The x-intercept is −1/Kₘ.

For the treated enzyme, Kₘ ≈ 0.06412 ppm and Vₘₐₓ ≈ 212.7 counts/min². The fitted intercepts are −15.60 and 0.004702.

The Michaelis–Menten equation

A Michaelis–Menten graph relates initial velocity to substrate concentration.

TreatedMichaelis–Menten0.00.51.01.5050100150200250[S] (ppm)v (counts/min²)KₘVₘₐₓ

v = Vmax[S] / (Km + [S])

Kₘ, the Michaelis–Menten constant, is the substrate concentration at half Vₘₐₓ. The Michaelis–Menten curve approaches Vₘₐₓ as substrate increases.

See Johnson and Goody (2011) for the original paper and its translation.

Kₘ and Vₘₐₓ: why use a nonlinear fit

This enzyme kinetics calculator fits the original rates to estimate Kₘ and Vₘₐₓ. A reciprocal transformation gives low-concentration measurements more influence. See Wilkinson (1961) for statistical estimation in enzyme kinetics.

Nonlinear fit

TreatedLineweaver–Burk−200204060−0.0050.0000.0050.0100.0150.0200.0251/[S] (ppm⁻¹)1/v (min²/count)1/Vₘₐₓ−1/Kₘ

Lineweaver–Burk regression

TreatedLineweaver–Burk−40−200204060−0.0050.0000.0050.0100.0150.0200.0251/[S] (ppm⁻¹)1/v (min²/count)1/Vₘₐₓ−1/Kₘ
MethodKₘVₘₐₓ
Nonlinear fit0.06412212.7
Lineweaver–Burk regression0.04841195.8

Enzyme inhibition on a Lineweaver–Burk plot

Compare conditions to see how inhibition changes apparent parameters.

Competitive

ControlCompetitiveLineweaver–Burk−505101520−0.020.000.020.040.061/[S] (mM⁻¹)1/v (min/µmol)

Pure noncompetitive

ControlNoncompetitiveLineweaver–Burk−505101520−0.050.000.050.101/[S] (mM⁻¹)1/v (min/µmol)

Uncompetitive

ControlUncompetitiveLineweaver–Burk−100102030−0.050.000.050.101/[S] (mM⁻¹)1/v (min/µmol)

Mixed

ControlMixedLineweaver–Burk−505101520−0.050.000.050.101/[S] (mM⁻¹)1/v (min/µmol)

Compare the intersection and the shifts in apparent parameters. These examples are illustrative.

TypeKₘVₘₐₓLine pattern
CompetitiveIncreasesUnchangedShared y-intercept
Pure noncompetitiveUnchangedDecreasesShared x-intercept
UncompetitiveDecreasesDecreasesParallel
MixedChangesDecreasesIntersect left of y-axis

Lineweaver–Burk plot FAQ

What does a Lineweaver–Burk plot show?

It plots 1/v against 1/[S]. The y-intercept is 1/Vₘₐₓ, the x-intercept is −1/Kₘ, and the slope is Kₘ/Vₘₐₓ.

Michaelis–Menten plot or Lineweaver–Burk plot: which should I use?

Use nonlinear fitting of the original rates to estimate parameters. A Lineweaver–Burk plot can help illustrate inhibition patterns.

Why are my Kₘ and Vₘₐₓ different from a Lineweaver–Burk regression?

Taking reciprocals magnifies errors at low substrate concentration, changing the relative influence of measurements.

What does the Michaelis–Menten equation mean?

Vₘₐₓ is the limiting rate and Kₘ is the substrate concentration at half Vₘₐₓ.

What units do Kₘ and Vₘₐₓ have in enzyme kinetics?

Kₘ has the units of substrate concentration and Vₘₐₓ has the units of velocity. Reciprocal axes use reciprocal units.

How do I tell competitive from noncompetitive inhibition?

Competitive inhibition produces lines sharing a y-intercept; pure noncompetitive inhibition shares an x-intercept. This tool does not classify inhibition automatically.

Can I fit sigmoidal allosteric enzyme kinetics?

No. Allosteric kinetics may require a Hill model, which this tool does not fit.

Is my data uploaded? What can I download?

Data stays in your browser. You can download SVG, PNG and a results CSV.

Make your Lineweaver–Burk plot

Fit your data and export a figure for your work.