Final answer:
Non-competitive inhibition occurs when an inhibitor binds to an allosteric site on the enzyme, changing its conformation and preventing effective substrate binding at the active site, which cannot be countered by increasing substrate concentration.
Step-by-step explanation:
In regards to the rules of non-competitive inhibition, the correct statement is that it alters the enzyme's conformation. Non-competitive inhibitors bind to an allosteric site on the enzyme, which is distinct from the active site, and induce a conformational change. This change affects the shape of the active site and prevents the substrate from binding effectively, impairing the enzyme's catalytic activity. Unlike competitive inhibitors, non-competitive inhibitors do not compete with the substrate for the active site, and their inhibitory effect cannot be overcome by increasing the concentration of the substrate.