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Enzymes work to speed up the rates of reaction. This is done by lowering the activation energy, or the energy needed to reach the transitition state. Activator increased the acitivity of enzymes while inhibitors decrease the activity of enzymes. Inhibitors can be classified as reversible or irreversible. Reversible inhibitors are changes to the enzyme that are not permanet. They include: competitive, uncompetitive, mixed, and noncompetitive (which are a type of mixed). Competitive inhibitor binds to the same place as the substrate, the active site. Inhibition can be overcome at high substrate concentrations. Vmax is not effected but Km increases. Uncompetitive inhibitors bind to the enzyme-substrate complex and cannot be overcome at high substrate concentration. Vmax and Km both decrease. Mixed and noncompetitive inhibitors can bind to the enzyme or the enzyme-substrate. They decrease the Vmax and do not change the Km. Irreversible inhibitors cannot be removed from the enzyme, instead the whole protein would have to be denatured to undo the changes made.