As we have seen, you can analyze the kinetic properties of a Michaelis enzyme by measuring its velocity of catalysis at a range of substrate concentrations and plotting [S] vs V, or 1/[S] vs 1/V. You can also analyze the properties of an enzyme inhibitor by carrying out the same experiment and graphic analysis in the presence of the inhibitor. If you do this for a noncompetitive inhibitor, what difference will you see when you compare the enzyme kinetics to an uninhibited control