This problem involves calculating the specific reaction velocity ($V$) for an enzymatic reaction using the Michaelis-Menten kinetic model. We are given the maximum reaction velocity ($V_{max}$), the Michaelis constant ($K_m$), and the substrate concentration ($[S]$).
The core equation relating these parameters is the Michaelis-Menten equation:
$ V = \frac{V_{max}[S]}{K_m + [S]} $
Where:
We are provided with the following values:
Substitute these values into the Michaelis-Menten equation:
$ V = \frac{(160 \, \mu mol/l.min) \times (40 \, \mu mol/l)}{(60 \, \mu mol/l) + (40 \, \mu mol/l)} $
The estimated velocity of the reaction at a substrate concentration of $40 \, \mu mol/l$ is $64 \, \mu mol/l.min$. This result aligns with the provided answer range.
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