What are the types of enzyme inhibition?

There are three main types of enzyme inhibition: competitive, noncompetitive, and uncompetitive inhibition. Each of these regulates enzyme activity in different ways.

1. In competitive inhibition, the enzyme inhibitor competes with the substrate for binding the active site of the enzyme. This occurs when a molecule other than the substrate, but with a similar structure and chemical composition, binds to the enzyme’s active site, directly preventing the substrate from binding. Because both the substrate and the inhibitor compete for the same binding site on the enzyme, increasing the substrate concentration can help overcome this type of inhibition. 
2. Noncompetitive inhibition occurs when the inhibitor binds to a site on the enzyme other than the active site, known as the allosteric site. When the inhibitor binds to the allosteric site, it doesn’t interfere with the substrate binding directly to the enzyme. However, it changes the shape of the enzyme’s active site, indirectly preventing the substrate from binding. In non-competitive inhibition, because the inhibitor is not in direct competition with the substrate, increasing substrate levels will not reverse the inhibitor’s action. 
3. In uncompetitive inhibition, the inhibitor binds only to the enzyme-substrate complex. It does not bind to the free enzyme and requires the formation of an enzyme-substrate complex. This type of enzyme inhibition is common in reactions that involve two or more products or substrates. This type of enzyme inhibition decreases both, the rate of substrate binding