This simulation plots rate data for Michaelis–Menten enzyme kinetics for four types of inhibition. For competitive inhibition, an inhibitor forms an inactive complex with the enzyme. For uncompetitive inhibition, an inhibitor forms an inactive complex with the enzyme-substrate complex. For mixed inhibition, the inhibitor forms both types of inactive complexes. For self-inhibition, the substrate itself inhibits the reaction by forming an inactive complex with the enzyme-substrate complex. Select “Michaelis–Menten” to plot the rate of substrate consumption versus substrate concentration. Select “Lineweaver–Burke” to plot -1/rate versus 1/(substrate concentration) so as to obtain a straight line (except for the self-inhibited case). The slope and intercept of this line are related to K_M, K_I, and V_max.  Use the slider to change the inhibitor concentration, which changes the slope and/or the y-intercept, depending on which type of inhibition is selected. When self-inhibited is selected, the substrate concentration is the inhibitor concentration, so the slider is hidden