Michaelis-Menten Equation Calculator
Calculate enzyme reaction velocity or the substrate concentration needed for a target rate.
About the Michaelis-Menten equation
Michaelis-Menten examples
These cases illustrate half-saturation and the approach toward maximum velocity.
| Inputs | Calculated value | Interpretation |
|---|---|---|
| [S] = 2.5 mM, Km = 0.5 mM, Vmax = 100 | v = 83.333 | Substrate is five times Km |
| [S] = 4 mM, Km = 4 mM, Vmax = 80 | v = 40.000 | Velocity is half of Vmax |
| v = 75, Km = 2 mM, Vmax = 100 | [S] = 6.000 mM | Inverse substrate calculation |
How to use the kinetics calculator
- Choose whether to solve for reaction velocity or substrate concentration.
- Enter Vmax and Km using consistent rate and concentration units.
- Enter substrate concentration or a target velocity, depending on the selected calculation.
- Select Calculate kinetics and interpret the result in the units supplied.
Frequently asked questions
What does Km mean?
Km is the substrate concentration predicted to produce half of Vmax in the Michaelis-Menten model. A lower Km often indicates half-saturation at a lower substrate concentration, but it is not always identical to binding affinity.
What does Vmax mean?
Vmax is the limiting initial reaction velocity when substrate is abundant relative to Km. Its value depends on enzyme concentration and assay conditions.
Why must target velocity be below Vmax?
The simple model approaches Vmax as substrate concentration increases but does not exceed or reach it at a finite concentration. Solving for a target at or above Vmax therefore has no finite physical answer.
Can I use micromolar instead of mM?
Yes, provided [S] and Km use the same concentration unit. The calculated substrate result will then be in that same unit.
Does this equation work for cooperative enzymes?
Not usually, because cooperative kinetics often produce a sigmoidal rather than hyperbolic rate curve. A Hill model or a mechanism-specific model may be more appropriate in that situation.