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Effect of different inhibitors on Km and Vmax

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Enzymes are biological catalysts that help to speed up the rate of reactions. All enzymes have two very important factors, Km and Vmax. V max is the maximum speed of the enzyme. Km is the concentration of substrate needed for the enzyme to work at half of its maximum speed. The lower the km, the better the enzyme is and the higher it's affinity for substrate is.

Inhibitors are molecules that inhibit or diminish the productivity of an enzyme. There are three different types of inhibitors.

Competitive inhibitor competes with the substrate for the active site on the enzyme. It resembles the substrate in it's shape and look. Competitive inhibition can be overcome if much more substrate is added that successfully outcompetes the inhibitor.

Competitive inhibitor does not change the Vmax on an enzyme but increases Km.

Uncompetitive inhibitors bind to the site on the enzyme other than the active site. The inhibitor will only bind to the enzyme that is already bound to the substrate and will stop the enzyme from creating product.

Uncompetitive inhibitor lowers Vmax and lowers Km.

Noncompetitive inhibitor can bind either enzyme alone or enzyme-substrate compels with equal affinity. Noncompetitive inhibitors do not alter Km but decrease Vmax.

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