The competitive inhibitor resembles the substrate and binds to the active site of the enzyme (Figure 8.15). The substrate is thereby prevented from binding to the same active site. A competitive inhibitor diminishes the rate of catalysis by reducing the proportion of enzyme molecules bound to a substrate.

Where does competitive binding occur?

During competitive inhibition, the inhibitor and substrate compete for the active site. The active site is a region on an enzyme to which a particular protein or substrate can bind. The active site will thus only allow one of the two complexes to bind to the site, either allowing a reaction to occur or yielding it.

Where does the inhibitor bind to the enzyme?

The competitive inhibitor binds to the active site and prevents the substrate from binding there. The noncompetitive inhibitor binds to a different site on the enzyme; it doesn't block substrate binding, but it causes other changes in the enzyme so that it can no longer catalyze the reaction efficiently.