Part of the Biology & Life Sciences suite · 39 calculators

Enzyme Kinetics Calculator

Reaction velocity from substrate concentration by the Michaelis–Menten equation — how far below Vmax the enzyme is running, and the substrate needed to reach any fraction of it.

Enzyme velocity rises with substrate concentration but saturates: v = Vmax × [S] / (Km + [S]).

Results update as you type
Results
Velocity (µmol/min)
46.1538
Share of Vmax
Regime
Substrate for the target fraction (µM)
Velocity at [S] = Km
Velocity at [S] = 10 Km
Vmax / Km
Velocity if substrate doubled
Reviewed September 2026. Biological arithmetic: identical everywhere, with no market variation of any kind. UK human genetics research is governed by the HFEA and HTA frameworks.
No account required · Google Analytics off unless allowedCalculator arithmetic runs in your browserResults update as you type
All calculations run 100% in your browser. The calculator code does not submit your figures to GlobalCalc to obtain a result.
About enzyme kinetics

How the enzyme kinetics calculator works

Enzyme velocity rises with substrate concentration but saturates: v = Vmax × [S] / (Km + [S]). At [S] equal to Km the enzyme runs at half speed; at ten times Km it is at 91%; it never quite reaches Vmax.

Km is the enzyme's affinity in disguise — a low Km means it is half-saturated at low substrate. The two parameters are what a Lineweaver–Burk or a direct fit extracts from the lab data.

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

Worked examples

InputsVelocity (µmol/min)Note
Substrate below Km46.153838% of Vmax
At Km60exactly half
Well above Km109.090991% — nearly saturated

Frequently asked questions

What is the Michaelis–Menten equation?

The rate law for an enzyme with a single substrate: velocity rises with substrate but saturates at Vmax because every active site is busy.

What does Km mean?

The substrate concentration at which the enzyme runs at half Vmax. A low Km means high affinity — the enzyme is saturated at low substrate.

Why does the velocity never reach Vmax?

Because there is always some fraction of free enzyme. Ten times Km gives 91%; a hundred times gives 99%.

How are Vmax and Km measured?

From velocity at several substrate concentrations, by non-linear fit or a Lineweaver–Burk plot. Modern practice fits directly; the double-reciprocal plot distorts the errors.

What is catalytic efficiency?

kcat over Km — how well the enzyme works at low substrate. Vmax over Km here is the same idea without the enzyme concentration.

Where these figures come from

Last checked: September 2026. Formulas are the standard textbook forms; assumptions are stated on each page because they are where these models break.