Allosteric inhibition focuses more on the usage of chemicals which alters the enzyme activity by binding at an allosteric site.
What is an allosteric inhibitor?
A drug that interacts with an enzyme at an allosteric site is known as an allosteric inhibitor.
The allosteric site is located differently than the active site. The inhibitor modifies the enzyme's three-dimensional shape.
Allosteric inhibitors alter the enzyme's active site in a way that lessens or prevents substrate binding.
In contrast, allosteric activators change the enzyme's active site to improve the enzyme's affinity for the substrate.
Non-competitive inhibitors always halt the active enzyme by forming a direct bond at a different location.
Allosteric inhibitors deactivate the enzyme to reduce enzymatic activity. A chemical that binds to the enzyme at an allosteric location is known as an allosteric inhibitor.