Question

competitive and non-competitive inhibition of enzyme function, and why it is important.

Answer 1

Answere :

Competitive inhibition :

It is a type of reversible inhibition where an inhibitor has to compete with a substrate to bind to an enzyme. This is because there is only one active site for the inhibitor to bind to.

Competitive Inhibitors mimic the substrate molecules and compete for the spot on the active site to control enzyme activity.

All non-regulatory enzymes show competitive inhibition. Clinically competitive enzyme inhibition is of great importance since most of the drugs act by competitive inhibition.

Example : Sulfa drug (sulfanilamide) kills bacteria during infection. It competes with the substrate molecule of paraaminobemic acid (PABA).

Non competitive inhibition :

It is a type of inhibition where an inhibitor binds to an allosteric site instead of an active so it does not compete with a substrate. The inhibitor's binding to the active site distorts the shape of the active site. Therefore, the substrate cannot bind to the active site anymore.

It is shown by regulatory enzymes, also called allosteric enzymes

Noncompetitive Inhibitors attaches to enzyme away from active site to change the shape of it. The substrate can no longer bind to the enzyme.

Example : The medicine, Lisinopril lowers high blood pressure. High blood pressure can occur because of angiotensin II overproduction. ACE enzyme catalyzes to the production of angiotensin II. When Lisinopril mediciation is taken, it lowers high blood pressure by inhibiting the ACE enzyme.