The value ${K_m}$ is the substrate concentration at which the rate of an enzyme-catalysed reaction is half its maximum rate, $\frac{{{V_{\max }}}}{2}$.
The ${K_m}$ was measured in the presence of a competitive inhibitor and in the presence of a
non-competitive inhibitor.
What could be the value of ${K_m}$ with inhibitor compared to the value of ${K_m}$ with no inhibitor?
1 )
A
2 )
B
C
4 )
D
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