Question

For a report, after plotting the lineweaver-burk plot for a protease enzyme with and without inhibitor. It shows that the km value increases in the presence of inhibitor and Vmax decreases. what type of inhibition is it? The inhibitor is an azide.

Answer 1

As the binding of inhibitor is affecting both ko and I Umane, (Km is increasing & - and u mare decreases most probe The this inhibition is mixed inhibition o 1 In mixed inhibition inhibitor can bind I to the enzyme in free form as a as substrate bound forno, but it will have more affinity for either free enzyme or substrate bound enzyme. Il es called mixed as it is a mix of both competitive and & uncompetitive inhibition. In competitive inhibition, inhibitor binds to the enzyme when substrate is not bound to enzyme and in uncompetitive inhibitor bindo only when substrate has been binded enzyme. Mixed inbibition decreases V mare of reaction, but Km value can increase or decrease in mixed inhibition. when mixed inhibition more closely resembles competitive binding on when inhibitor binds to o enzyme in free form ( enzyme not bound to substraten there is increase in km value. e affinity of enyme for substrate decreases with so the km value increases)