The inhibitor which closely resembles the substrate in its molecular structure and inhibits the enzyme activity by biniding to the active site of the enzyme is called

Options

A. feedback inhibitor
B. non-competitive inhibitor
C. competitive inhibitor
D. allosteric modulator.

Answer

C

Explanation

In competitve inhibition, the inhibitor (l) closely resembles the real substrate (S), and is regarded as a substrate analogue. The inhibitor competes with substrate and binds at the active site of the enzyme but does not undergo any catalysis. As long as the competitive inhibitor to bind. A competitive inhibitor diminishes the rate of catalysis by reducing the proportion of enzyme molecules bound to a substrate. At any given inhibitor concentration, competitve inhibition can be relieved by increasing the substrate concentration. Under these conditions, the substrate successfully competes with the inhibitor for the active site. Thus, competitive inhibition is usually reversible since the addition of more substrate tends to reduce the effect of the inhibitor. In competitive inhibition, the reduce the effect of the inhibitor. In competitve inhibition, the `K_(m)` value increases whereas `V_(max)` remains unchanged.