Different between reversible inhibitor and non reversible inhibitor and their functions?
Reversible inhibitors can bind to and dissociate from the enzyme, while irreversible inhibitors form strong covalent bonds with the enzyme, rendering it permanently inactive.
Reversible inhibitors can be competitive, non-competitive, or uncompetitive, depending on where they bind to the enzyme. Competitive inhibitors bind to the active site of the enzyme, competing with the substrate for binding. Non-competitive inhibitors bind to a site other than the active site, changing the shape of the enzyme and preventing the substrate from binding. Uncompetitive inhibitors bind only to the enzyme-substrate complex.
Irreversible inhibitors form covalent bonds with the enzyme, usually at the active site, leading to permanent inhibition of the enzyme. This can be useful in some cases, such as certain medications that target specific enzymes in disease-causing organisms. However, irreversible inhibitors can also be harmful if they bind to essential enzymes in the human body.
Overall, reversible inhibitors are generally preferred over irreversible inhibitors in drug development due to their ability to be easily controlled and reversed.