Final answer:
When an inhibitor binds to an enzyme at a location other than the active site, causing a conformational change that reduces enzyme activity, it's called non-competitive or allosteric inhibition. The inhibitor attaches to the allosteric site, and this interaction can either decrease or increase enzyme activity, depending on whether the molecule is an inhibitor or an activator.
Step-by-step explanation:
When an inhibitor binds to an enzyme at a site other than the active site, this process is called non-competitive inhibition or allosteric inhibition. The site where the inhibitor binds is known as the allosteric site. By binding to this site, the inhibitor causes a conformational change in the enzyme. As a result, the shape of the enzyme's active site is altered, which decreases its ability to bind the substrate, reducing enzyme activity irrespective of the concentration of substrate present. It's important to note that allosteric inhibitors and allosteric activators can bind to the allosteric site; while inhibitors decrease enzyme activity, activators increase the affinity of the enzyme for its substrate.