Question:

$K_m$ and $V_{max}$ of an enzyme preparation are 5 µM and 30 $µM min^{-1}$ respectively. Considering, $K_i$ value of competitive inhibitor is 60 µM, the velocity ($V_0$) of this enzyme-catalyzed reaction in the presence of 200 µM of substrate and 600 µM of competitive inhibitor is _______ $ µM min^{-1}$ (rounded off to two decimal places).

Updated On: Nov 18, 2025
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Correct Answer: 23.5

Solution and Explanation

To solve this problem, we determine the reaction velocity ($V_0$) using the formula for enzyme kinetics in the presence of a competitive inhibitor. The modified Michaelis-Menten equation for competitive inhibition is:

V0 = (Vmax * [S]) / (Km * (1 + [I]/Ki) + [S])

 

Given:

  • $V_{max} = 30 \mu M \ min^{-1}$
  • $K_m = 5 \mu M$
  • $K_i = 60 \mu M$
  • [S] = 200 µM
  • [I] = 600 µM

First, calculate the factor by which $K_m$ is increased due to the inhibitor:

Km,app = Km * (1 + [I]/Ki) = 5 * (1 + 600/60) = 5 * (1 + 10) = 55 µM

 

Now use the modified Michaelis-Menten equation:

V0 = (30 * 200) / (55 + 200)

 

= 6000 / 255

 

≈ 23.53 µM min-1

 

The calculated velocity is 23.53 µM min-1.

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