An enzymatic reaction exhibits Michaelis–Menten kinetics. What will happen if the concentration of enzyme is doubled keeping \( [S_0] \gg [E] \)?
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In Michaelis–Menten kinetics, increasing enzyme concentration increases \( V_{max} \), but \( K_m \) remains constant as it is an intrinsic property of the enzyme-substrate complex.
\( V_{max} \) will increase; \( K_m \) will remain same
\( K_m \) will increase; \( V_{max} \) will remain same
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The Correct Option isC
Solution and Explanation
Step 1: Recall Michaelis–Menten equation:
\[
V = \frac{V_{max}[S]}{K_m + [S]}
\]
Here, \( V_{max} = k_{cat}[E] \), where \( [E] \) is the enzyme concentration and \( k_{cat} \) is the turnover number. Step 2: Analyze what happens when enzyme concentration \([E]\) is doubled:
If enzyme concentration is doubled, \( V_{max} \) also doubles because it is directly proportional to \([E]\).
However, \( K_m \) is a constant that depends on the enzyme-substrate interaction and is not affected by enzyme concentration. Step 3: Use condition \( [S_0] \gg [E] \):
This ensures we are in the range where Michaelis–Menten assumptions apply and substrate saturation is sufficient for the reaction rate to approach \( V_{max} \).