Compared with the uninhibited enzyme, a non competitive inhibitor

Explanation

Because the inhibitor binds elsewhere and cannot be displaced by substrate, a fraction of the enzyme is permanently out of action, so the maximum achievable rate falls while the affinity of the remaining active sites for the substrate is unaltered. A competitive inhibitor shows the opposite pattern, an unchanged Vmax with an apparently raised Km. This pair of effects is the standard way of telling the two kinds apart in the laboratory.