Final answer:
An allosteric inhibitor binds to an enzyme away from the active site, inducing a conformational change that decreases substrate affinity and inhibits enzyme activity.
Step-by-step explanation:
An allosteric inhibitor is a molecule that binds to an enzyme at an allosteric site, which is different from the active site where substrate molecules normally bind. This allosteric binding causes a conformational change in the enzyme, modifying the active site of the enzyme in such a way that the affinity for the substrate decreases, making the active site less accommodating for the substrate.
This alteration prevents the substrate from binding as efficiently to the enzyme, effectively inhibiting the enzyme's catalytic activity.