Which of these statements about enzyme-catalyzed reactions is false? 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. The Michaelis-Menten constant Km equals the [S] at which V = 1/2 Vmax: O At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. The rate of a reaction decreases steadily with time as substrate is depleted. O If enough substrate is added, the normal Vmax of a reaction can be attained even in the presence of a competitive inhibitor.
Which of these statements about enzyme-catalyzed reactions is false? 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. The Michaelis-Menten constant Km equals the [S] at which V = 1/2 Vmax: O At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. The rate of a reaction decreases steadily with time as substrate is depleted. O If enough substrate is added, the normal Vmax of a reaction can be attained even in the presence of a competitive inhibitor.
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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![Which of these statements about enzyme-catalyzed reactions is false?
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.
The Michaelis-Menten constant Km equals the [S] at which V = 1/2 V,
max:
At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme
concentration.
The rate of a reaction decreases steadily with time as substrate is depleted.
If enough substrate is added, the normal V,
of
max
a reaction can be attained even in the presence of a
competitive inhibitor.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Ffbfd0029-e037-4bef-a6dc-2fab8c35ba69%2Fae3fb3e7-eb87-4d7f-83c0-ec6470d1e473%2Fdfoy1ho_processed.png&w=3840&q=75)
Transcribed Image Text:Which of these statements about enzyme-catalyzed reactions is false?
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.
The Michaelis-Menten constant Km equals the [S] at which V = 1/2 V,
max:
At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme
concentration.
The rate of a reaction decreases steadily with time as substrate is depleted.
If enough substrate is added, the normal V,
of
max
a reaction can be attained even in the presence of a
competitive inhibitor.
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