Which effect on enzymatic reaction rate is caused by competitive inhibitor concentration increasing toward substrate concentration?

💡 Explanation

When competitive inhibitor concentration increases toward the substrate concentration, the inhibitor competes for the enzyme's active site, increasing the apparent Michaelis constant (Km), but the maximum reaction rate (Vmax) remains unaffected, because at very high substrate concentrations, the substrate can still displace the inhibitor and achieve Vmax. Therefore, Vmax remains unchanged, rather than Km approaching zero or altered kinetic parameters, which would require different inhibition mechanisms.

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