The presence of the competitive inhibitor decreases the Km of the enzyme for the substrate.
A competitive inhibitor reacts reversibly with the enzyme to form an enzyme-inhibitor complex.
In competitive inhibition the inhibitor molecule is not chemically changed by the enzyme.
The competitive inhibitor does not affect the rate of breakdown of the enzyme-substrate complex.
Competitive inhibition is a type of enzyme inhibition in which the inhibitor binds to the active site on the enzyme. This prevents binding of the substrate to the enzyme and hence affects the rate of breakdown of the enzyme-substrate complex. Competitive inhibitors bind reversibly to the active site of the enzyme to form an enzyme-inhibitor complex. In this, the maximum velocity (Vmax) is unchanged while Km is increased as inhibitor interferes with the binding of substrate and this inhibition can be overcome by increasing the substrate concentration. In this, the inhibitor molecule is not chemically changed by the enzyme. Thus, the correct answer is option D. The statement 'The competitive inhibitor does not affect the rate of breakdown of the enzyme-substrate complex' is incorrect because the inhibitor binding to the active site directly prevents the formation of the enzyme-substrate complex, thereby affecting its breakdown rate.