Differentiate reversible and irreversible inhibitors ?

Reversible inhibitors are substances that bind to an enzyme and can be easily removed from the enzyme, allowing the enzyme to regain its activity. There are two types of reversible inhibitors:

1. Competitive inhibitors: These inhibitors compete with the substrate for binding to the active site of the enzyme. They bind reversibly to the active site and can be displaced by increasing the substrate concentration. Competitive inhibitors do not affect the maximum velocity (Vmax) of the enzyme, but increase the apparent Michaelis-Menten constant (Km).

2. Non-competitive inhibitors: These inhibitors bind to a site on the enzyme other than the active site, known as the allosteric site. They do not compete with the substrate for binding and can bind to both the free enzyme and the enzyme-substrate complex. Non-competitive inhibitors decrease the maximum velocity (Vmax) of the enzyme, but do not affect the apparent Michaelis-Menten constant (Km).

On the other hand, irreversible inhibitors are substances that bind to an enzyme and permanently inactivate it. Irreversible inhibitors form covalent bonds with the enzyme, resulting in a permanent alteration of the enzyme's structure or active site. Irreversible inhibitors cannot be easily removed from the enzyme and the enzyme cannot regain its activity.