13. In an enzyme-substrate reaction, the reaction is favoured because 1elag ulomon3 A. The transition state of the reaction is de-stabilized. B. The transition state of the reaction is stabilized. C. The activation energy of the reaction is increased. D. The free energy of the reaction to yield products is modified. E. The reaction becomes more exothermic. MKA 14. In enzyme kinetics, the turnover number, kcat, is A. Equivalent to the dissociation constant of the enzyme-substrate complex. B. The amount of enzyme available to bind substrate per unit time at the maximum velocity. C. The amount of substrate transformed per unit time when [S] is low. D. Half the value of the Michaelis constant, KM. The amount of substrate transformed per unit time at the maximum velocity.
13. In an enzyme-substrate reaction, the reaction is favoured because 1elag ulomon3 A. The transition state of the reaction is de-stabilized. B. The transition state of the reaction is stabilized. C. The activation energy of the reaction is increased. D. The free energy of the reaction to yield products is modified. E. The reaction becomes more exothermic. MKA 14. In enzyme kinetics, the turnover number, kcat, is A. Equivalent to the dissociation constant of the enzyme-substrate complex. B. The amount of enzyme available to bind substrate per unit time at the maximum velocity. C. The amount of substrate transformed per unit time when [S] is low. D. Half the value of the Michaelis constant, KM. The amount of substrate transformed per unit time at the maximum velocity.
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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![13. In an enzyme-substrate reaction, the reaction is favoured because
elag lulomon
A. The transition state of the reaction is de-stabilized.
B. The transition state of the reaction is stabilized.
C. The activation energy of the reaction is increased.
D. The free energy of the reaction to yield products is modified.
E. The reaction becomes more exothermic.
14. In enzyme kinetics, the turnover number, kcat, is
A. Equivalent to the dissociation constant of the enzyme-substrate complex.
B. The amount of enzyme available to bind substrate per unit time at the maximum
velocity.
C. The amount of substrate transformed per unit time when [S] is low.
D. Half the value of the Michaelis constant, KM.
E. The amount of substrate transformed per unit time at the maximum velocity.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F1ea64ab9-a648-4310-b850-7545b4e1f826%2Fb531fa7e-6d4d-45e4-be6f-8359b8066bca%2F9qmt2g_processed.jpeg&w=3840&q=75)
Transcribed Image Text:13. In an enzyme-substrate reaction, the reaction is favoured because
elag lulomon
A. The transition state of the reaction is de-stabilized.
B. The transition state of the reaction is stabilized.
C. The activation energy of the reaction is increased.
D. The free energy of the reaction to yield products is modified.
E. The reaction becomes more exothermic.
14. In enzyme kinetics, the turnover number, kcat, is
A. Equivalent to the dissociation constant of the enzyme-substrate complex.
B. The amount of enzyme available to bind substrate per unit time at the maximum
velocity.
C. The amount of substrate transformed per unit time when [S] is low.
D. Half the value of the Michaelis constant, KM.
E. The amount of substrate transformed per unit time at the maximum velocity.
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