Question

Why does the inhibitor compete with the substrate in enzymes?

Answer 1

Competitive inhibition:

1. Competitive inhibition is the disruption of a chemical pathway as a result of one chemical substance competing with another for binding or bonding, hence inhibiting the action of the other.
2. A molecule with which an enzyme interacts is known as a substrate.
3. A substrate is put into the active site of the enzyme, which is where weak bonds between two molecules might form.
4. For instance, the competitive inhibitor penicillin prevents the active site of an enzyme used by many bacteria to build their cells.
5. Drugs and natural substrates compete for an enzyme's active site attachment.
6. These medications are known as competitive inhibitors.
7. Some medications do not bind to the active site of the enzyme.
8. These bind to an enzyme's allosteric site, which is a separate binding location.
9. The geometry of the active site is altered by the binding of the inhibitor at the allosteric site, rendering the substrate unable to recognize it.
10. As a result, it competes with the natural substrate for attachment to enzyme active sites during competitive inhibition and does not bind to allosteric sites.