A) The inhibitor binds to the substrate.
B) The inhibitor can be overcome with sufficiently high concentrations of substrate.
C) The inhibitor reacts with a critical residue of the enzyme.
D) The inhibitor binds to the same active site as the substrate.
E) The KM is smaller in the presence of inhibitor.
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Multiple Choice
A) catalysis of substrate to product
B) binding of substrate
C) removal of product(s) from active site
D) prevention of enzyme inhibition
E) None of the answers is correct.
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Multiple Choice
A) turnover number
B) Michaelis constant
C) dissociation constant
D) rate constant
E) None of the answers is correct.
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Multiple Choice
A) holoenzyme
B) coenzyme
C) isozyme
D) apoenzyme
E) None of the answers is correct.
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Multiple Choice
A) competitive
B) noncompetitive
C) mixed
D) uncompetitive
E) None of the answers is correct.
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Multiple Choice
A) reaction at equilibrium
B) irreversible reaction
C) spontaneous reaction
D) exergonic reaction
E) endergonic reaction
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Multiple Choice
A) 150 mM
B) 0.15 mM
C) 150 M
D) 1.5 nM
E) 15000 pM
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Multiple Choice
A) at equilibrium
B) nonspontaneous
C) spontaneous
D) irreversible
E) None of the answers is correct.
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Multiple Choice
A) increasing the probability of product formation
B) shifting the reaction equilibrium
C) stabilization of transition state
D) All of the answers are correct.
E) None of the answers is correct.
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Multiple Choice
A) allosteric modulation
B) transition state enhancement
C) sequential binding
D) induced fit
E) None of the answers is correct.
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Multiple Choice
A) The enzyme is saturated with substrate.
B) Most of the enzyme does not have substrate bound.
C) There is more enzyme than substrate.
D) All of the answers are correct.
E) None of the answers is correct.
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