The Michaelis-Menten equation for competitive inhibition is given by:
\[
V = \frac{V_{\text{max}} [S]}{K_m(1 + [I]/K_i) + [S]}
\]
where:
- \( V \) is the observed velocity,
- \( V_{\text{max}} \) is the maximum velocity,
- \( [S] \) is the substrate concentration,
- \( K_m \) is the Michaelis constant,
- \( [I] \) is the concentration of the inhibitor,
- \( K_i \) is the dissociation constant of the enzyme-inhibitor pair.
For half-maximal velocity, \( V = \frac{V_{\text{max}}}{2} \), so the equation simplifies to:
\[
\frac{V_{\text{max}}}{2} = \frac{V_{\text{max}} [S]}{K_m(1 + [I]/K_i) + [S]}
\]
Simplifying further:
\[
1 = \frac{[S]}{K_m(1 + [I]/K_i) + [S]}
\]
We know that the half-maximal velocity occurs at a substrate concentration of \( [S] = 0.5 \times 10^{-6} \, \text{M} \) without the inhibitor, and at \( [S] = 1.5 \times 10^{-6} \, \text{M} \) with the inhibitor. Hence, for the condition with the inhibitor, we use the fact that the half-maximal velocity corresponds to:
\[
1 = \frac{1.5 \times 10^{-6}}{0.5 \times 10^{-6}(1 + [I]/K_i) + 1.5 \times 10^{-6}}
\]
Given \( K_i = 2 \times 10^{-7} \, \text{M} \), solving for \( [I] \), we get:
\[
[I] \approx 0.4 \, \mu M
\]
Thus, the concentration of the competitive inhibitor is approximately \( 0.4 \, \mu M \).