Enzymes get faster with more substrate — but only up to a point. Watch the rate climb and then flatten at Vmax as the enzyme saturates.
Michaelis–Menten Enzyme KineticsLive
how enzymes saturate
Controls
Presets
Enzymes speed reactions but saturate: as substrate rises, the rate approaches a ceiling Vmax. Km — the substrate level giving half Vmax — measures how tightly the enzyme binds. Low Km means high affinity. Educational tool.
Reading this result: At [S] near Km (5 mM) the enzyme works at about half speed (50% of Vmax) — this is the steepest, most substrate-sensitive part of the curve.
Runs locally in your browser — free forever. Scale to the cloud when reality gets heavy.
★ Sign in to save this setupSave your tuned setup, or drop this simulation into your own site, docs, or course page.
How it works
The Michaelis–Menten equation, v = Vmax·[S]/(Km + [S]), describes how enzyme rate saturates with substrate. Vmax is the maximum rate; Km, the substrate concentration giving half Vmax, measures binding affinity — lower Km means the enzyme grabs substrate more tightly. Educational tool.
✦
Ask the AI about this model
The math, the assumptions, real-world uses, or a code translation — explained for this exact simulation.
Is this michaelis menten calculator tool really free?▾
Yes. Michaelis–Menten Kinetics runs entirely in your browser using your device's own compute, so local use is free forever. You only pay Compute Tokens if you scale a job to the cloud.
Do I need to install anything?▾
No. Everything runs client-side in a modern browser — no downloads, no license, no account required to start.
Can I save or share my simulation?▾
Create a free account to save projects, and use a shareable embed or minted DOI to publish a live, interactive version anywhere.
How accurate are the results?▾
The solver uses established numerical methods, but results are for research and educational purposes and should be validated against experiment or professional review before you rely on them.