Final answer:
Competitive inhibitors bind to the active site, not elsewhere, so the answer to the question is false. Non-competitive inhibitors bind to an allosteric site and affect enzyme activity by altering the shape of the active site.
Step-by-step explanation:
The question is whether a competitive inhibitor binds at a site other than the active site. The answer is False. A competitive inhibitor binds directly to the active site of an enzyme, thereby competing with the substrate for the same site. Conversely, a non-competitive inhibitor binds to an allosteric site, which is a different location on the enzyme, not the active site. This binding results in a conformational change that affects the enzyme's active site and hinders the binding of the substrate. Non-competitive inhibitors can attach to the enzyme whether the substrate is already bound or not.
In summary, competitive inhibitors do not bind to an allosteric site but rather to the active site, directly competing with the substrate, whereas non-competitive inhibitors bind to an allosteric site impacting the active site indirectly.