Study Guide for Campbell Biology
11th Edition
ISBN: 9780134443775
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece, Martha R. Taylor, Michael A. Pollock
Publisher: PEARSON
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Chapter 8, Problem 12TYK
Summary Introduction
Introduction: Enzymes are biological protein catalysts that alter the
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What is true about a competitive inhibitor of an enzyme? You can choose more than one
a. it binds the active site
b. it binds an allosteric site
c. it physically blocks the substrate
d. it warps the active site
e. it can be overcome with large amounts of substrate
An inhibitor that reversibly binds to a site other than the enzyme's active site is called a(n)
a. noncompetitive inhibitor
b. competitive inhibitor
c. antagonisitc inhibitor
d. antibiotic
When an enzyme catalyzes a reaction… A. The pH changes B. Substrate concentration is reduced C. Product concentration is reduced D. Substrate concentration is increased
Chapter 8 Solutions
Study Guide for Campbell Biology
Ch. 8 - Complete the following concept map that summarizes...Ch. 8 - Complete the following table to indicate how the...Ch. 8 - Develop a concept map on free energy and G. The...Ch. 8 - Prob. 4IQCh. 8 - Prob. 5IQCh. 8 - In the following graph of an exergonic reaction...Ch. 8 - In the following diagram of a catalytic cycle,...Ch. 8 - Return to the diagram in Interactive Question 3.7,...Ch. 8 - Both ATP and ADP serve as regulators of enzyme...Ch. 8 - What is the relationship between the concept of...
Ch. 8 - What role do enzymes play in metabolism?Ch. 8 - ________ the totality of an organisms chemical...Ch. 8 - _______ pathways that use energy to synthesize...Ch. 8 - Prob. 3TYKFCh. 8 - _______ the most random form of energyCh. 8 - _______ term for the measure of disorder or...Ch. 8 - Prob. 6TYKFCh. 8 - _______ inhibitors that decrease an enzymes...Ch. 8 - Prob. 8TYKFCh. 8 - Prob. 9TYKFCh. 8 - Prob. 10TYKFCh. 8 - Catabolic and anabolic pathways are often coupled...Ch. 8 - Which statement most closely reflects the first...Ch. 8 - When a cell breaks down glucose, only about 34% of...Ch. 8 - Prob. 4TYKCh. 8 - Prob. 5TYKCh. 8 - Prob. 6TYKCh. 8 - One way in which a cell maintains metabolic...Ch. 8 - Prob. 8TYKCh. 8 - Prob. 9TYKCh. 8 - What is meant by an induced fit? a. The binding of...Ch. 8 - In an experiment, changing the pH from 7 to 6...Ch. 8 - Prob. 12TYKCh. 8 - Penicillin binds to the active site of an enzyme...Ch. 8 - Prob. 14TYKCh. 8 - Prob. 15TYKCh. 8 - Which line in the diagram indicates the G of the...Ch. 8 - Prob. 17TYKCh. 8 - Prob. 18TYKCh. 8 - Prob. 19TYKCh. 8 - Prob. 20TYK
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- An enzyme has the ability to catalyze reactions of several unrelated compounds. The mechanism of how this enzyme operates is best explained by a. the lock-and-key theory b. the induced-fit theory c. the enzyme-substrate complex d. the efficiency of the enzymearrow_forwardWhich of the following is incorrect about enzyme inhibitors? a. They can be reversible or irreversible b. The irreversible inhibitors form a covalent bond with the enzyme C. Some irreversible inhibitors are called suicide inhibitors d. Aspirin is an example of a reversible inhibitorarrow_forwardAn allosteric inhibitor does which of the following? a. Binds to an enzyme away from the active site and changes the conformation of the active site, increasing its affinity for substrate binding. b. Binds to the active site and blocks it from binding substrate. c. Binds to an enzyme away from the active site and changes the conformation of the active site, decreasing its affinity for the substrate. d. Binds directly to the active site and mimics the substrate.arrow_forward
- Indicate whether each of the following statements describes a reversible competitive inhibitor, a reversible noncompetitive inhibitor, or an irreversible inhibitor. More than one answer may apply.a. Both inhibitor and substrate bind at the active site on a random basis.b. The inhibitor effect cannot be reversed by the addition of more substrate.c. Inhibitor structure does not have to resemble substrate structure.d. The inhibitor and substrate can bind to the enzyme simultaneouslyarrow_forwardWhich of the following statements about Competitive and noncompetitive inhibition is false? a. A noncompetitive inhibitor does not change the Km of the enzyme. b. A competitive inhibitor does not change the Vmax of the enzyme c. The noncompetitive inhibitor can bind either free enzyme or the enzyme–substrate complex. d.A competitive inhibitor decreases the apparent Km for a given substrate.arrow_forwardWhich ONE of the following would be most effective as a feedback mechanism for anenzymatic reaction? A. Reduced concentration of the product B. A change in pH C. Increased concentration of substrate D. Temporary binding of a non-substrate molecule in the active binding sitearrow_forward
- When an enzymatic reaction is in progress, do you expect to see happen to the amount of substrate? A It will increase as the reaction proceeds. B It will decrease as the reaction proceeds. C The amount will not change as reaction proceeds. D It is not possible to predict what will happen to it as the reaction proceeds.arrow_forwardAll of the following are accurate about enzymes except: A. Enzymes are typically globular proteins with an active site B. Enzymes decrease activation energy C. Enzymes can be used over and over to catalyze a substrate to a product D. Enzymes are versatile and can catalyze different types of chemical reactionsarrow_forwardWhich of the following best describes the relationship between an enzyme and a substrate a. stable b. causes permanent alteration to the enzyme c. results from non-complimentary bonding d. are complimentaryarrow_forward
- Potassium cyanide is a poison which combines with cytochrome A3 to prevent binding of oxygen to the enzyme without altering the Km of the reaction with respect to reduced cytochrome c. Which type of inhibition does this represent? c. Competitive inhibition D. Uncompetitive inhibition A. Irreversible inhibition B. Noncompetitive inhibition 10. Which of the following enzyme classes catalyze reactions in which two molecules become dissociated from each other? A. Kinase В. Нydrolase C. Isomerase D. Ligase 11. Which of the following enzyme classes catalyze reactions in which two molecules become covalently linked to each other? C. Isomerase D. Ligase A. Kinase В. Нydrolasearrow_forwardWhich of the following accurately describes how an enzyme functions? a. reduces the energy content of the products b. allows for the exothermic reaction of materials that are usually endothermic c. changes the reaction mechanism effectively reducing the activation energy d. shifts the equilibrium for the reactionarrow_forwardIn a highly high-temperature environment, you placed an enzyme and some substrates. You've seen that there hasn't been any reaction. Applying what you have learned on enzyme activity, how would you explain what occurred? A. The enzyme was not placed at a pH level that would allow it to react at its maximum rate. B. There are not enough enzymes for the reaction to occur. C. The enzyme may have denatured or broken down due to the high temperature of the environment, resulting in no reaction. D. There are not enough substrates for reaction to occur. Substrate concentration affects enzyme activity. Determine what would occur when there are too many substrates and fewer enzymes? A. No enzyme activity would occur. B. The reaction rate would continuously increase. C. The reaction would speed up tremendously. D. Maximal rate of reaction would occur. Enzyme activity mainly involves the active site and the substrate. How would you compare the active site from the substrate? A. The substrate…arrow_forward
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