This problem requires calculating the Michaelis constant ($K_m$) for an enzyme using the Michaelis-Menten equation and the provided reaction parameters.
The relationship between initial velocity ($V_0$), maximum velocity ($V_m$), substrate concentration ($[S]$), and the Michaelis constant ($K_m$) is given by the Michaelis-Menten equation:
$ V_0 = \frac{V_m [S]}{K_m + [S]} $
To find $K_m$, we can rearrange the Michaelis-Menten equation:
$ V_0 (K_m + [S]) = V_m [S] $
$ V_0 K_m + V_0 [S] = V_m [S] $
$ V_0 K_m = V_m [S] - V_0 [S] $
$ V_0 K_m = [S] (V_m - V_0) $
$ K_m = \frac{[S] (V_m - V_0)}{V_0} $
Now, substitute the given values into the rearranged equation:
$ K_m = \frac{(1.0 \times 10^{-4} \text{ M}) (75 \text{ nmol } l^{-1} \text{ min}^{-1} - 60 \text{ nmol } l^{-1} \text{ min}^{-1})}{60 \text{ nmol } l^{-1} \text{ min}^{-1}} $
Perform the calculation:
$ K_m = \frac{(1.0 \times 10^{-4} \text{ M}) (15 \text{ nmol } l^{-1} \text{ min}^{-1})}{60 \text{ nmol } l^{-1} \text{ min}^{-1}} $
$ K_m = (1.0 \times 10^{-4} \text{ M}) \times \frac{15}{60} $
$ K_m = (1.0 \times 10^{-4} \text{ M}) \times 0.25 $
$ K_m = 0.25 \times 10^{-4} \text{ M} $
$ K_m = 2.5 \times 10^{-5} \text{ M} $
The calculated $K_m$ value is $2.5 \times 10^{-5}$ M.
The graph below shows the activity of enzyme pepsin in the presence of inhibitors aliphatic alcohols (P) or N-acetyl-1-phenylalanine (Q). Which ONE of the following represents the nature of inhibition by P and Q, respectively?

The following plot represents the Lineweaver-Burk equation of an enzymatic reaction both in the presence and the absence of inhibitor. Here, V is the velocity of reaction and S is the substrate concentration.

The nature of inhibition shown in the plot is