As described by the equation above, at high concentrations of substrate, "V""0" approaches "V""max"/α'. Thus, an uncompetitive inhibitor lowers the measured "V""max". Apparent "K""m" also decreases, because required to reach one-half "V""max" decreases by the factor α'. It is important to note that V"max" and K"m" decrease at the same rate as a result of the inhibitor. This is apparent when viewing a Lineweaver-Burk plot of uncompetitive enzyme inhibition: the ratio between V and K"m" remains the same with or without an inhibitor present.