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Question

An enzyme of 40 kDa is added to a substrate solution in a molar ratio of 1:3. The concentration of the enzyme in the mixture is 12 mg/ml. What would be the corresponding substrate concentration?

The correct answer is
0.9 mM

Enzyme Concentration Calculation: Determining Substrate Molarity

This solution calculates the substrate concentration based on the given enzyme concentration, molecular weight, and molar ratio.

Enzyme Concentration Conversion

  1. Convert the enzyme molecular weight (MW) from kDa to g/mol:

    MWenzyme = 40 kDa = 40,000 g/mol

  2. Convert the enzyme concentration from mg/ml to g/L:

    Enzyme Concentration = 12 mg/ml = 12,000 mg/L = 12 g/L

  3. 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

Substrate Concentration Calculation

  1. Use the given molar ratio of enzyme to substrate (1:3):

    $ \frac{\text{Molarity}_\text{enzyme}}{\text{Molarity}_\text{substrate}} = \frac{1}{3} $

  2. 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.

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Important Questions from Enzyme Kinetics Michaelis Menten K_m V_{max}

  1. An enzyme following Michaelis-Menten kinetics, catalyses a reaction with an initial velocity ($V_0$) of $2\ \mu\text{M s}^{-1}$ at the substrate concentration of $10\ \mu\text{M}$. If the turnover number ($k_{\text{cat}}$) of the enzyme for the given substrate is $500\ \text{s}^{-1}$ and the enzyme concentration in the reaction is $0.01\ \mu\text{M}$, then the value of the Michaelis-Menten constant ($K_m$) would be__________ $\times\ 10^{-6}\ \text{M}$ (in integer).
  2. 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? 

  3. 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

  4. For an enzyme catalyzed reaction, the plot that correctly represents the relationship between the rate and temperature is
  5. In an enzyme catalyzed reaction, the initial reaction velocity is only one fourth of its maximum velocity. If the substrate concentration is $3.0 \times 10^{-3}$ mM, the value of $K_m$ in micro molar ($\mu$M) will be ....
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