An enzyme has a $K_m$ of $4.7 \times 10^{-5} \text{ M}$ and $V_m$ is $22 \text{ micro moles per litre per min}$. The enzyme reaction is carried out at a substrate concentration of $2 \times 10^{-4} \text{ M}$. The initial reaction velocity for this enzyme catalyzed reaction will be
This problem involves calculating the initial reaction velocity ($v$) of an enzyme-catalyzed reaction using the Michaelis-Menten equation. We are given the Michaelis constant ($K_m$), the maximum velocity ($V_{max}$), and the substrate concentration ($[S]$).
The Michaelis-Menten equation relates the initial reaction velocity ($v$) to the maximum velocity ($V_{max}$), the substrate concentration ($[S]$), and the Michaelis constant ($K_m$):
$v = \frac{V_{max}[S]}{K_m + [S]}$
$v = \frac{(22 \text{ micromoles per litre per min}) \times (2 \times 10^{-4} \text{ M})}{(4.7 \times 10^{-5} \text{ M}) + (2 \times 10^{-4} \text{ M})}$
$V_{max}[S] = 22 \times (2 \times 10^{-4}) = 44 \times 10^{-4} = 4.4 \times 10^{-3}$
Convert $K_m$ to the same power of 10 as $[S]$ for easier addition:
$K_m = 4.7 \times 10^{-5} \text{ M} = 0.47 \times 10^{-4} \text{ M}$
$K_m + [S] = (0.47 \times 10^{-4}) + (2 \times 10^{-4}) = 2.47 \times 10^{-4} \text{ M}$
$v = \frac{4.4 \times 10^{-3}}{2.47 \times 10^{-4}} \text{ micromoles per litre per min}$
$v \approx 17.81 \text{ micromoles per litre per min}$
The calculated velocity is approximately $17.8 \text{ micromoles per litre per min}$.
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