Worked enzyme-kinetics example

Do not linearize to fit.

The Lineweaver–Burk plot turns a curve into a straight line, and the straight line looks excellent: r² = 0.998. It also moves Vmax by 12% and Km by 23% against the same six measurements.

6 substrate concentrations1–50 µMTwo fitting routes7-minute read

The problem

A transformation that fixes the geometry breaks the errors.

The Michaelis–Menten model, v = Vmax·[S] / (Km + [S]), is a curve. Before nonlinear regression was routine, the standard move was to plot 1/v against 1/[S], read Vmax from the intercept and Km from the slope, and fit by eye or by least squares. The algebra is exact. The statistics are not: taking reciprocals compresses the high-concentration points and stretches the low-concentration ones, so the fit is dominated by the measurements with the least information and the largest relative error.

The measurements

[Substrate] (µM) 1 2 5 10 20 50
Velocity 12 20 38 55 72 90

Six concentrations spanning a fiftyfold range, one reading each. The velocity is still climbing at 50 µM, which matters later.

The same six points, two fitting routes

Route Vmax Km (µM) Fit quality
Nonlinear regression on v vs [S] 105.106 (SE 1.548) 8.872 (SE 0.369) R² = 0.99913
Lineweaver–Burk (1/v vs 1/[S]) 92.459 6.820 r² = 0.99766

The double-reciprocal route reports a Vmax 12.0% lower and a Km 23.1% lower than the direct fit — and it reports them with an r² that would pass any informal quality check. r² is computed in reciprocal space, where it describes how well a line fits transformed numbers, not how well the model fits the measurements.

Practical rule: fit the model on the scale you measured. Use nonlinear regression on v against [S], and treat the Lineweaver–Burk plot as a display convention or a diagnostic for inhibition patterns — not as the estimator.

Residuals from the direct fit

In velocity units, in concentration order: +1.354, +0.666, +0.117, −0.692, −0.807, +0.735. They change sign, stay small relative to velocities of 12 to 90, and show no systematic sweep — which is what supports the model here, far more than R² = 0.99913 does on its own.

What Km and Vmax actually claim

Km is the substrate concentration at which velocity reaches half of Vmax; it is a concentration, reported in the units of [S], not a rate and not an affinity constant in general. Vmax is an extrapolated ceiling: the velocity the model predicts at infinite substrate. Neither is measured directly here. With the highest concentration at 50 µM and a fitted Km of 8.872 µM the series does reach roughly 5.6 × Km, so Vmax is reasonably constrained — but a design whose top concentration sits near or below Km makes Vmax an extrapolation the data cannot support, and Km inherits that uncertainty.

Limit: single readings at six concentrations give the standard errors above under the model's own assumptions, with no independent estimate of measurement error. Replicate each concentration if the constants are the result you intend to report. Nothing on this page establishes that Michaelis–Menten is the right model for your enzyme — cooperativity, substrate inhibition and non-steady-state conditions all produce curves this shape will fit badly, and the residuals are where you would see it.

A defensible kinetics workflow

  1. Choose concentrations that bracket the expected Km, ideally spanning well below to several multiples above it.
  2. Replicate each concentration; single readings cannot separate model error from measurement error.
  3. Fit v against [S] directly by nonlinear regression. Do not fit a transformed variable.
  4. Inspect residuals against [S] for systematic curvature before reading either constant.
  5. Report Km with its units and Vmax with its uncertainty, and state the concentration range the estimates rest on.

What Plotwright checks

Both fits above come from the engine's regression routes — the same nonlinear machinery used for dose–response curves, which carries reference checks on the validation page. Every value on this page is reproducible from the six visible measurements in the linked editable project.

Sources and reproducibility

  1. Johnson, K. A. & Goody, R. S. (2011), “The Original Michaelis Constant: Translation of the 1913 Michaelis–Menten Paper”, Biochemistry—the original derivation with modern commentary on how the constants are defined and estimated.
  2. IC50 and EC50 dose response—the same nonlinear-fitting discipline applied to sigmoidal potency curves.
  3. Standard curves and interpolation—the related trap of judging a fit by r² instead of its residuals.
  4. Plotwright statistical validation—published expected values, numerical tolerances and evidence limits.

Fit the curve you measured.

Plotwright keeps the raw velocities, the nonlinear fit, its residuals and the editable figure in one inspectable project.