This solution calculates the substrate concentration based on the given enzyme concentration, molecular weight, and molar ratio.
Convert the enzyme molecular weight (MW) from kDa to g/mol:
MWenzyme = 40 kDa = 40,000 g/mol
Convert the enzyme concentration from mg/ml to g/L:
Enzyme Concentration = 12 mg/ml = 12,000 mg/L = 12 g/L
Calculate the molar concentration (molarity) of the enzyme:
Molarity = Concentration (g/L) / MW (g/mol)
Enzyme Molarity = $ \frac{12 \text{ g/L}}{40,000 \text{ g/mol}} $ = 0.0003 mol/L
Enzyme Molarity = 0.3 mmol/L = 0.3 mM
Use the given molar ratio of enzyme to substrate (1:3):
$ \frac{\text{Molarity}_\text{enzyme}}{\text{Molarity}_\text{substrate}} = \frac{1}{3} $
Calculate the substrate molarity:
Molaritysubstrate = Molarityenzyme $ \times $ 3
Molaritysubstrate = 0.3 mM $ \times $ 3 = 0.9 mM
The corresponding substrate concentration is 0.9 mM.
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