Difference between reversible and irreversible inhibitors?

Answer 1

Enzyme inhibitors are molecules that bind to enzymes and decrease their activity. The binding of an inhibitor can stop a substrate from entering the enzyme's active site and/or hinder the enzyme from catalyzing its reaction. Inhibitor binding is either reversible or irreversible. Irreversible inhibitors usually react with the enzyme and change it chemically. These inhibitors modify key amino acid residues needed for enzymatic activity. In contrast, reversible inhibitors bind non-covalently and different types of inhibition are produced depending on whether these inhibitors bind the enzyme, the enzyme-substrate complex, or both.

Answer 2

Reversible inhibitors bind to enzymes temporarily and can be displaced from the enzyme, allowing the enzyme to function once the inhibitor is removed. Irreversible inhibitors form permanent bonds with the enzyme, leading to a permanent loss of enzyme activity.