K

FIGURE 6-15 Three types of reversible inhibition. (a) Competitive inhibitors bind to the enzyme's active site. (b) Uncompetitive inhibitors bind at a separate site, but bind only to the ES complex. KI is the equilibrium constant for inhibitor binding to E; K{ is the equilibrium constant for inhibitor binding to ES. (c) Mixed inhibitors bind at a separate site, but may bind to either E or ES.

FIGURE 6-15 Three types of reversible inhibition. (a) Competitive inhibitors bind to the enzyme's active site. (b) Uncompetitive inhibitors bind at a separate site, but bind only to the ES complex. KI is the equilibrium constant for inhibitor binding to E; K{ is the equilibrium constant for inhibitor binding to ES. (c) Mixed inhibitors bind at a separate site, but may bind to either E or ES.

ply by adding more substrate. When [S] far exceeds [I], the probability that an inhibitor molecule will bind to the enzyme is minimized and the reaction exhibits a normal Vmax. However, the [S] at which V0 = 2 Vmax, the apparent Km, increases in the presence of inhibitor by the factor a. This effect on apparent Km, combined with the absence of an effect on Vmax, is diagnostic of competitive inhibition and is readily revealed in a double-reciprocal plot (Box 6-2). The equilibrium constant for inhibitor binding, KI, can be obtained from the same plot.

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