Irreversible inhibitors usually react with the enzyme and change it chemically (e.g. via covalent bond formation). In contrast, reversible inhibitors bind non-covalently and different types of inhibition are produced depending on whether these inhibitors bind to the enzyme, the enzyme-substrate complex, or both. Penicillin irreversibly inhibits the enzyme transpeptidase by reacting with a serine residue in the transpeptidase. This reaction is irreversible and so the growth of the bacterial cell wall is inhibited. An irreversible inhibitor will bind to an enzyme so that no other enzyme-substrate complexes can form. It will bind to the enzyme using a covalent bond at the active site which therefore makes the enzyme denatured. An example of an irreversible inhibitor is diisopropyl fluorophosphates which is present in nerve gases.

Shivangi Ojha

130 resources

0

0

0

Like