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Question

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

The correct answer is
$17.8 \text{ micro moles per litre per min}$

Enzyme Kinetics: Calculating Initial Velocity

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 ($[S]$).

Michaelis-Menten Equation

The Michaelis-Menten equation relates the initial reaction velocity ($v$) to the maximum velocity ($V_{max}$), the substrate concentration ($[S]$), and the Michaelis constant ($K_m$):

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

Given Values

  • Michaelis constant, $K_m = 4.7 \times 10^{-5} \text{ M}$
  • Maximum velocity, $V_{max} = 22 \text{ micromoles per litre per min}$
  • Substrate concentration, $[S] = 2 \times 10^{-4} \text{ M}$

Calculation Steps

  1. Substitute values into the Michaelis-Menten equation:

    $v = \frac{(22 \text{ micromoles per litre per min}) \times (2 \times 10^{-4} \text{ M})}{(4.7 \times 10^{-5} \text{ M}) + (2 \times 10^{-4} \text{ M})}$

  2. Calculate the numerator:

    $V_{max}[S] = 22 \times (2 \times 10^{-4}) = 44 \times 10^{-4} = 4.4 \times 10^{-3}$

  3. Calculate the denominator ($K_m + [S]$):

    Convert $K_m$ to the same power of 10 as $[S]$ for easier addition:

    $K_m = 4.7 \times 10^{-5} \text{ M} = 0.47 \times 10^{-4} \text{ M}$

    $K_m + [S] = (0.47 \times 10^{-4}) + (2 \times 10^{-4}) = 2.47 \times 10^{-4} \text{ M}$

  4. Calculate the initial velocity ($v$):

    $v = \frac{4.4 \times 10^{-3}}{2.47 \times 10^{-4}} \text{ micromoles per litre per min}$

    $v \approx 17.81 \text{ micromoles per litre per min}$

  5. Round to the nearest option:

    The calculated velocity is approximately $17.8 \text{ micromoles per litre per min}$.

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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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