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Although this is a simple analogy, small molecules inside the cells of your body, called enzymes, serve a similar function by making and breaking apart other molecules. A catalyst is something that increases the speed of a reaction.
The substrate is the name for the substance an enzyme works on.
The substrate binds to the active site, or the place on the enzyme that actually does the work.
Enzymes work at different speeds depending on their environment.
The rate at which the enzyme does its job is called enzyme activity.
They change the shape of the enzyme, like allosteric inhibitors, but they make the enzyme better able to bind the substrate, instead of worse. These molecules and their allosteric sites are like the 'on switch' for the enzyme.
Next, let's look at a few examples of how allosteric inhibitors and activators affect the allosteric site and enzyme activity.In our analogy, you are like the enzyme and the Legos are like the substrate.You grab the substrate and change it, either putting pieces together or breaking them apart.We'll also go over some examples of allosteric regulation in the body.Have you ever played with Legos or building blocks as a kid?These molecules and the allosteric site to which they bind are like the 'off switch' for the enzyme.Allosteric activators on the other hand, make the enzyme more efficient.These molecules bind the allosteric site and change the confirmation, or shape, of the enzyme.Molecules that turn off enzymes are called allosteric inhibitors.There are two forms of hemoglobin, the T state (or tense state), which makes hemoglobin bind oxygen less tightly, and the R state (or relaxed state), which makes hemoglobin bind oxygen more tightly.Now, this might give you the impression that the T state is bad since it prevents hemoglobin from binding oxygen.