<u>Allosteric regulation</u> occurs when a molecule binds the enzyme on another site other than the active site activating or inhibiting it.
<h3>What is allosteric regulation?</h3>
Allosteric regulation occurs when molecules bind to the enzyme on another side, which is not the binding site. This is the <u>allosteric site</u>.
Allosteric molecules can be either,
- Allosteric inhibitors → inhibit the enzyme activity by not letting the substrate get attached to the enzyme.
Allosteric inhibition is non-competitive inhibition because the allosteric molecule does not compete directly with the substrate.
It attaches to the enzyme at another site, impeding the substrate to bind the enzyme and turning off its function.
- Allosteric activators → change the active site and make it more efficient to bind the substrate.
Allosteric activation is a cooperative process in which the enzyme function is enhanced. Some substrates can even work as allosteric activators for other active binding sites.
Allosteric enzymes can change their conformation, exhibiting active and inactive conformations as a result of substrate binding at the activated center and regulatory molecules at other binding sites -allosteric centers-.
You can learn more about allosteric regulation at
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