A competitive inhibitor binds at a site other than the active site. irreversibly binds and inactivates the enzyme. cannot be processed by the enzyme. binds to and inactivates the substrate. does not inhibit enzyme activity but does lower substrate concentration.

Answer: irreversibly binds and inactivates the enzyme.

Explanation: An enzyme can be defined as any substance that binds substrates in a manner that facilitates the formation of product.

These are nonspecific factors that would inactivate any enzyme. The activity of enzymes can also be regulated by more specific inhibitors. A competitive inhibitor can be defined as an inhibitors bind reversibly at the active site of an enzyme.

It is important to note the difference:

An irreversible inhibitor inactivates an enzyme by bonding covalently to a particular group at the active site. The inhibitor-enzyme bond is so strong that the inhibition cannot be reversed by the addition of excess substrate.

A reversible inhibitor inactivates an enzyme through noncovalent, more easily reversed, interactions. Unlike an irreversible inhibitor, a reversible inhibitor can dissociate from the enzyme. Reversible inhibitors include competitive inhibitors and noncompetitive inhibitors.