Question 33 Which statement is a TRUE description of a transition state inhibitor of an enzyme? a. They bind covalently to the enzyme. b. They bind to the enzyme more tightly than the substrate. c. They react irreversibly with the enzyme. d. They require the presence of a stable functional group to mimic the functionality in the transition state. e. All of the above are true. Question 34 Allosteric enzymes have which of the following characteristics: a. Their catalytic activity cannot be regulated. O b. They conform to Michaelis-Menton kinetics. O c. They have multiple active sites that display cooperativity. d. They have regulatory molecules that only stimulate enzyme activity. e. They have a hyperbolic dependence of the reaction velocity with substrate concentration.

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Questions 33,34

Question 33
Which statement is a TRUE description of a transition state inhibitor of an enzyme?
O a. They bind covalently to the enzyme.
b. They bind to the enzyme more tightly than the substrate.
O c. They react irreversibly with the enzyme.
d. They require the presence of a stable functional group to mimic the functionality in the
transition state.
e. All of the above are true.
Question 34
Allosteric enzymes have which of the following characteristics:
O a. Their catalytic activity cannot be regulated.
O b. They conform to Michaelis-Menton kinetics.
O c. They have multiple active sites that display cooperativity.
d. They have regulatory molecules that only stimulate enzyme activity.
e. They have a hyperbolic dependence of the reaction velocity with substrate concentration.
Transcribed Image Text:Question 33 Which statement is a TRUE description of a transition state inhibitor of an enzyme? O a. They bind covalently to the enzyme. b. They bind to the enzyme more tightly than the substrate. O c. They react irreversibly with the enzyme. d. They require the presence of a stable functional group to mimic the functionality in the transition state. e. All of the above are true. Question 34 Allosteric enzymes have which of the following characteristics: O a. Their catalytic activity cannot be regulated. O b. They conform to Michaelis-Menton kinetics. O c. They have multiple active sites that display cooperativity. d. They have regulatory molecules that only stimulate enzyme activity. e. They have a hyperbolic dependence of the reaction velocity with substrate concentration.
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