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FREE · LOCAL ANALYSIS

Michaelis–Menten Enzyme Kinetics

Vmax · Km · nonlinear fit quality

Transparent modelExample dataLocal processingReview methodology →
ADVANCED ANALYSIS · RUO

Michaelis–Menten Enzyme Kinetics

Vmax · Km · nonlinear fit quality

Calculated locally in this browser

Column order: substrate_concentration, initial_rate

Editable data table
substrate_concentrationinitial_rate
Paste CSV / TSV

Analysis result

Vmax2.538
Km0.484
0.9998
Valid rows6

Model assumes simple Michaelis–Menten behavior without substrate inhibition or cooperativity.

Research use only. Validate raw data, exclusions and interpretation against the approved analysis plan.

INPUT FORMAT

Data requirements

Enter at least 4 positive substrate and initial-rate pairs.

substrate_concentration, initial_rate
INTERPRETATION

Review before reporting

Research use only. Validate raw data, exclusions and interpretation against the approved analysis plan.

Check raw observations, excluded rows, model assumptions and study-specific acceptance criteria before using the result.

METHOD

Transparent analysis

Inputs are processed locally in your browser. Review the calculation policy, limitations and verification approach before reporting a result.

Read the methodology →