Inhibitors decrease the rates that enzymes bind to substrates and convert them to products. Three types of inhibition (competitive, uncompetitive, noncompetitive/mixed) and reaction with no inhibitor are compared for an enzyme reaction that obeys Michaelis–Menten kinetics. Substrate concentration is plotted versus time for a continuous stirred-tank reactor (CSTR) and for a batch reactor. Change the inhibitor concentration, which remains constant during reaction, with a slider. Set the substrate feed concentration with a slider. Select "inhibition type" to see the reaction steps, pathways, and a brief description of the type of inhibition. In competitive inhibition, the inhibitor attacks the enzyme to form an enzyme-inhibitor complex ; adding more substrate minimizes the inhibitor effect. In uncompetitive inhibition, the inhibitor attacks the enzyme-substrate complex ; adding more substrate does not overcome this type of inhibition since the inhibitor does not compete with the substrate for the enzyme sites. In noncompetitive inhibition, the inhibitor attacks the enzyme to form an enzyme-inhibitor complex or it attacks the enzyme-substrate complex to form an enzyme-substrate-inhibitor complex .