Final answer:
An inhibitor binding to an enzyme typically decreases enzyme activity by preventing substrate binding or altering the enzyme's conformation, which ultimately slows down or stops the chemical reaction.
Step-by-step explanation:
The effect of an inhibitor binding to an enzyme often results in the decrease of the enzyme's activity. Inhibitors can function in a variety of ways. For instance, a competitive inhibitor competes with the substrate for the active site of the enzyme, blocking it and preventing substrate binding. On the other hand, a noncompetitive inhibitor binds to an allosteric site, changing the conformation of the enzyme and thus reducing its affinity for the substrate. An irreversible inhibitor binds covalently to the active site, permanently inhibiting the enzyme's function. It is important to note that the binding of an inhibitor does not necessarily degrade nor activate the enzyme, nor does it result in the complex being transported out of the cell.
An inhibitor is a molecule that interferes with the function of an enzyme, either by slowing or stopping the chemical reaction. When an inhibitor binds to an enzyme, it can have different effects depending on the type of inhibitor. In the case of a noncompetitive inhibitor, it binds to an enzyme away from the active site and changes the conformation of the active site, decreasing its affinity for the substrate. This ultimately leads to a decrease in enzyme activity. Therefore, the correct answer is b) Decreases enzyme activity.