Michaelis-Menten Calculator
Calculate the rate of a Michaelis-Menten enzyme at a substrate concentration, or the substrate for a target rate, with the saturation curve and rates at multiples of Km.
Formula
- the maximum rate, reached at saturating substrate
- the substrate concentration at which the rate is half of Vmax
- substrate concentration, in the same unit as Km
How it works
For a single-substrate enzyme at steady state, the rate rises with substrate concentration and levels off at Vmax. The Michaelis constant Km is the concentration that gives half of it, and is a rough measure of how tightly the enzyme binds its substrate: a smaller Km means half-saturation at a lower concentration.
The table shows how the rate climbs with multiples of Km: at Km the enzyme is 50% saturated, at ten times Km about 91%, and getting near Vmax takes much more. That is why assays designed to measure Vmax use a substrate concentration of at least ten times Km.
Worked example
An enzyme with Vmax = 100 and Km = 2.5 (any consistent units) at [S] = 5.
- v = 100 × 5 / (2.5 + 5) = 66.67.
- [S] is 2 × Km, so the enzyme is 66.7% saturated.
v = 66.67, which is 66.7% of Vmax. To reach v = 75 would need [S] = 7.5.
These are the values the calculator opens with, so you can check its output against this example.
Assumptions
- One substrate, no inhibition, cooperativity or product inhibition.
- The substrate is in large excess over the enzyme, so its concentration is unchanged during the measurement.
- Steady state: the enzyme-substrate complex forms and breaks down at the same rate.
Common mistakes
- Using the equation for an allosteric or cooperative enzyme, whose curve is sigmoidal.
- Mixing units for [S] and Km.
- Expecting to reach Vmax at a finite concentration. The rate only approaches it.
Related tools
Related equipment
Service documentation, failure modes and parts for the instruments this calculation is used with.