Answer:
1. A competitive inhibitor exhibits a composition, which is identical to the substrate that can combine with the enzyme just like the substrate.
2. A noncompetitive inhibitor combines with the enzyme that is not the active site.
3. Generally, a irreversible inhibitor produces a covalent bond with an amino acid group within the active site that inhibits the substrate from entering the active site or inhibits catalytic activity.
4. The competitive inhibitor competes with the substrate for the active site present on the enzyme.
5. When the noncompetitive inhibitor gets combined with an enzyme, the shape of the enzyme gets distorted.
6. The enzyme inhibitors disrupts the usual associations between an enzyme and its substrate.