Explore the Enzyme Kinetics Laboratory
Change substrate, enzyme, temperature, pH and inhibitors, and watch a live Michaelis-Menten curve. Free, no signup, runs in your browser.
- Free to use
- No signup
- Nothing to install
- Runs in your browser
Illustration. Open the tool for the real thing.
See it in action
The Enzyme Kinetics Laboratory with sample data entered and the result showing.
What is the Enzyme Kinetics Laboratory?
Change substrate, enzyme, temperature, pH and inhibitors, and watch a live Michaelis-Menten curve - then switch to a Lineweaver-Burk plot to estimate Vmax and Km yourself. It runs in your browser, so a change to a setting or a drag on an object shows up at once.
Drug designers use exactly this kind of kinetics to test whether a new medicine competitively or noncompetitively blocks a disease-related enzyme.
3 steps to your result
Open the tool and follow along. Nothing to install.
What you get
The Michaelis-Menten equation v = Vmax[S] / (Km + [S]) describes how reaction rate depends on substrate concentration.
Km is the substrate concentration where the reaction runs at half its maximum rate.
A competitive inhibitor raises the apparent Km but leaves Vmax unchanged; a noncompetitive inhibitor lowers Vmax but leaves Km unchanged.
Push temperature past the enzyme's optimum and watch the rate collapse.
Add a competitive inhibitor and watch Km rise on the curve.
Switch to Lineweaver-Burk and estimate Vmax and Km from the intercepts, then check your answer.
Used for
Pick one to see how it fits.
Biology learners
Biology students and teachers who want to explore living systems, populations and genetics interactively and safely.
Try it freeTeachers
For teachers: project the Enzyme Kinetics Laboratory on the board, let students predict the result, then run it together and test this: Add a competitive inhibitor and watch Km rise on the curve. For students: change one thing at a time and write down what changes.
Try it freeHow it compares
A plain look at this tool next to the usual alternative.
| This simulation | Textbook diagram | |
|---|---|---|
| Interactive | Drag, tap and change settings | Fixed picture |
| Install | Nothing to install | Not needed |
| Cost | Free to use | Depends on the book |
Questions people ask
What does Km actually mean?
It measures how much substrate is needed to reach half-maximal reaction rate - a small Km means the enzyme binds substrate tightly.
How can you tell competitive from noncompetitive inhibition from a graph?
On a Lineweaver-Burk plot, competitive inhibition changes the x-intercept (Km) but keeps the same y-intercept (Vmax); noncompetitive inhibition changes the y-intercept but keeps the same x-intercept.
Is the Enzyme Kinetics Laboratory free to use?
Yes. The Enzyme Kinetics Laboratory is free, needs no signup or download and runs in your web browser. It is part of the Biology group of AZRS simulations.
Does the Enzyme Kinetics Laboratory work on a phone or tablet?
Yes. The Enzyme Kinetics Laboratory takes touch input as well as mouse input, so you can use its 9 adjustable settings with a finger. A larger screen makes the controls and graphs easier to read.
How do I use the Enzyme Kinetics Laboratory?
1. In the Enzyme Kinetics Laboratory, use the controls to change Substrate concentration, Enzyme concentration, Temperature, pH, Inhibitor type, and more. The simulation reacts instantly. 2. In the Enzyme Kinetics Laboratory, pick an option such as None, Competitive, Noncompetitive, Michaelis-Menten to switch modes or load an example. 3. In the Enzyme Kinetics Laboratory, press "Check my estimate", "Load mystery inhibitor", "Submit answer" to start, reset or change what is happening. 4. Start with this experiment: Push temperature past the enzyme's optimum and watch the rate collapse. Drag any glowing handle, object or slider with your mouse or finger and the Enzyme Kinetics Laboratory responds in real time. 5. Change one setting at a time and watch which readout moves, then compare it with this idea: The Michaelis-Menten equation v = Vmax[S] / (Km + [S]) describes how reaction rate depends on substrate concentration.
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Change substrate, enzyme, temperature, pH and inhibitors, and watch a live. Free to use.
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