All Exams Test series for 1 year @ ₹349 only
Question

The Lineweaver-Burk plot of an enzymatic reaction shows $V_{max}$ of $160 \, \mu mol/l.min$ and $k_m$ of $60 \, \mu mol/l$. For a substrate concentration of $40 \, \mu mol/l$, the velocity of the reaction is estimated to be __________ $\mu mol/l.min$.

Enzymatic Reaction Velocity Calculation

This problem involves calculating the specific reaction velocity ($V$) for an enzymatic reaction using the Michaelis-Menten kinetic model. We are given the maximum reaction velocity ($V_{max}$), the Michaelis constant ($K_m$), and the substrate concentration ($[S]$).

Michaelis-Menten Equation

The core equation relating these parameters is the Michaelis-Menten equation:

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

Where:

  • $V$ is the reaction velocity at a given substrate concentration.
  • $V_{max}$ is the maximum velocity when the enzyme is saturated with substrate.
  • $K_m$ is the substrate concentration at which the reaction velocity is half of $V_{max}$.
  • $[S]$ is the substrate concentration.

Applying the Given Values

We are provided with the following values:

  • $V_{max} = 160 \, \mu mol/l.min$
  • $K_m = 60 \, \mu mol/l$
  • $[S] = 40 \, \mu mol/l$

Substitute these values into the Michaelis-Menten equation:

$ V = \frac{(160 \, \mu mol/l.min) \times (40 \, \mu mol/l)}{(60 \, \mu mol/l) + (40 \, \mu mol/l)} $

Calculation Steps

  1. Calculate the numerator: $V_{max} \times [S]$ $ 160 \times 40 = 6400 $
  2. Calculate the denominator: $K_m + [S]$ $ 60 + 40 = 100 $
  3. Divide the numerator by the denominator to find $V$: $ V = \frac{6400}{100} $ $ V = 64 \, \mu mol/l.min $

Result

The estimated velocity of the reaction at a substrate concentration of $40 \, \mu mol/l$ is $64 \, \mu mol/l.min$. This result aligns with the provided answer range.

Was this answer helpful?

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 ....
Need Expert Advice?

Start Your Preparation with Prepp Mobile App

Download the app from Google Play & App Store
Download the app from Google Play & App Store
Prepp Mobile App