The value $K_m$ is the substrate concentration at which the rate of an enzyme-catalysed reaction is half of the maximum rate, $\frac{V_{\max}}{2}$. The $K_m$ was determined in the presence of a competitive inhibitor and in the presence of a non-competitive inhibitor. What might the value of $K_m$ with inhibitor be compared with the value of $K_m$ with no inhibitor?
- Acompetitive inhibitor: less; non-competitive inhibitor: less
- Bcompetitive inhibitor: less; non-competitive inhibitor: more
- Ccompetitive inhibitor: more; non-competitive inhibitor: less
- Dcompetitive inhibitor: the same; non-competitive inhibitor: more