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Question

For a single substrate enzyme, a reaction is carried out at a substrate concentration four times the value of $K_m$. The observed initial velocity will be __________ % of $V_{max}$.

Enzyme Kinetics: Initial Velocity Calculation

This solution details the calculation of the initial reaction velocity ($v_0$) relative to the maximum velocity ($V_{max}$) for an enzyme-catalyzed reaction. The calculation is performed under specific conditions where the substrate concentration ([S]) is four times the Michaelis constant ($K_m$).

Michaelis-Menten Equation Fundamentals

The core principle governing enzyme kinetics under these conditions is the Michaelis-Menten equation:

$ v_0 = \frac{V_{max}[S]}{K_m + [S]} $

This equation relates the initial reaction velocity ($v_0$) to the maximum possible velocity ($V_{max}$), the substrate concentration ([S]), and the enzyme's affinity for the substrate, represented by $K_m$.

Applying the Specific Substrate Concentration

The problem specifies that the substrate concentration is four times the $K_m$. This can be written as:

$ [S] = 4 K_m $

Step-by-Step Velocity Calculation

Substitute the given substrate concentration into the Michaelis-Menten equation:

  1. Replace $[S]$ with $4 K_m$ in the equation:

    $ v_0 = \frac{V_{max}(4 K_m)}{K_m + (4 K_m)} $

  2. Simplify the denominator:

    $ v_0 = \frac{V_{max}(4 K_m)}{5 K_m} $

  3. Cancel the $K_m$ terms:

    $ v_0 = \frac{4}{5} V_{max} $

Determining Velocity as a Percentage of $V_{max}$

To express the initial velocity as a percentage of $V_{max}$, calculate the fraction $\frac{v_0}{V_{max}}$ and multiply by 100%:

$ \frac{v_0}{V_{max}} = \frac{4}{5} $

$ \text{Percentage of } V_{max} = \frac{4}{5} \times 100\% = 0.8 \times 100\% = 80\% $

Final Result

Under the condition where the substrate concentration is four times the $K_m$, the observed initial velocity ($v_0$) is 80% of the maximum velocity ($V_{max}$).

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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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