Which of these statements about enzyme-catalyzed reactions is false? At saturated levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme A concentration. B If enough substrate is added, the reaction can reach Vmax even in the presence of a competitive inhibitor. The rate of a reaction decreases steadily with time as the substrate is depleted. The activation energy for the catalyzed reaction is the same as for the uncatalyzed reaction, but the equilibrium constant is more favorable in the enzyme-catalyzed reaction. E The Michaelis-Menten constant Km equals the [S] at which V = 1/2 Vmax.

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Chapter1: Biochemistry: An Evolving Science
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Which of these statements about enzyme-catalyzed reactions is false?
At saturated levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme
A
concentration.
B If enough substrate is added, the reaction can reach Vmax even in the presence of a competitive inhibitor.
The rate of a reaction decreases steadily with time as the substrate is depleted.
The activation energy for the catalyzed reaction is the same as for the uncatalyzed reaction, but the
equilibrium constant is more favorable in the enzyme-catalyzed reaction.
E The Michaelis-Menten constant Km equals the [S] at which V = 1/2 Vmax.
Transcribed Image Text:Which of these statements about enzyme-catalyzed reactions is false? At saturated levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme A concentration. B If enough substrate is added, the reaction can reach Vmax even in the presence of a competitive inhibitor. The rate of a reaction decreases steadily with time as the substrate is depleted. The activation energy for the catalyzed reaction is the same as for the uncatalyzed reaction, but the equilibrium constant is more favorable in the enzyme-catalyzed reaction. E The Michaelis-Menten constant Km equals the [S] at which V = 1/2 Vmax.
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