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.

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.

Introductory Chemistry: An Active Learning Approach

6th Edition

ISBN:9781305079250

Author:Mark S. Cracolice, Ed Peters

Publisher:Mark S. Cracolice, Ed Peters

Chapter22: Biochemistry

Section: Chapter Questions

Problem 22.3TC

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Similar questions

. Describe the lock-and-key model for enzymes. Why are the shapes of the enzyme and its substrate important in this model? What does it mean to say that an enzyme is inhibited by a particular molecule? What happens if this inhibition is irreversible? Can you think of a situation in which it might be advantageous to be able to inhibit an enzyme?
In the multienzyme sequence shown below, molecules of D are able to fit to the enzyme E1 and prevent the conversion of A to B. What is this action of E called? AE1BE2CE3D a. effector inhibition b. allosteric inhibition c. feedback inhibition d. competitive inhibition by nonproduct
Compare the lock-and-key and induced-fit models for substrate binding to an enzyme.
Describe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.
The human body has an average pH of about 7 and a temperature of about 37C. Use graphs to illustrate enzyme activity in the human body as a function of the following: a. Substrate concentration b. Enzyme concentration c. pH include pH optimum value d. Temperature include temperature optimum value
Based on the graphical information in Problem 21-41 about enzymes A and B a. What is the optimum pH for enzyme B? b. What is the optimum temperature for enzyme A? c. Which enzyme has the greater activity at a pH of 7.2? d. Which enzyme has the greater activity at a temperature of 37.2C?
The site on an enzyme molecule that does the catalytic work is called the: a. binding site. b. allosteric site. c. lock. d. active site.
Based on the graphical information in Problem 21-41 about enzymes A and B indicate whether the enzyme activity of enzyme B increases or decreases when the following changes in reaction conditions are made. a. pH decreases from 7.6 to 7.2 b. pH increases from 7.2 to 7.4 c. temperature decreases from 37.8C to 37.6C d. temperature increases from 38.2C to 38.4C
Describe the importance of zymogens in the body. Give an example of an enzyme that has a zymogen.
. How does the efficiency of an enzyme compare with that of inorganic catalysts? Are enzymes more or less efficient?
Match the following enzymes and substrates: Enzyme Substrate a. sucrase b. amylase c. lactase d. maltase e. arginase maltose amylose sucrose arginine lactose
Write a brief description of the relationships among each of the following groups of terms or phrases. Answers to the Concept-Linking Exercises are given at the end of the chapter. Enzyme, enzyme substrate, active site, induced fit model