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 20TYK
Summary Introduction
Introduction: Enzyme is defined as a biological catalyst that speeds up
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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. Нydrolase
What is the reason why the transition state of a catalyzed reaction is lower has lower energy compared to an uncatalyzed reaction?
A. because enzymes only work at low temperatures
B. because of favorable interactions with the substrate
C. because of enthalpic interactions between the enzyme and the transition state
D. A and B
The mechanism in which the end product of a metabolic pathway inhibits an either step in the pathway is known as
A. Reversible inhibition
B. Metabolic inhibition
C. Feedback inhibition
D. Allosteric inhibition
E. Noncoopetative inhibition
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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- What is the definition of a catabolic metabolic pathway? A. A pathway that releases energy and releases matter B. A pathway that stores energy and releases matter C. A pathway that releases energy and stores matter D. A pathway that stores energy and stores matterarrow_forwardWhat distinguishes a linear metabolic pathway from a cyclic metabolic pathway? A. The last step of the pathway regenerates a reactant for the first step. B. The product inhibits an enzyme in the pathway, slowing or stopping the metabolic pathway. C. A linear pathway runs straight in one direction from reactant to product. D. Enzymes convert reactants into intermediates before separate enzymes convert intermediates into products.arrow_forwardWhich of the following is true about allosteric enzymes? A. Allosteric enzymes are always multimeric. B. Regulatory sites (allosteric sites) on an allosteric enzyme are always different from the catalytic site. C. Allosteric enzymes always change the conformation of the active site in response to binding of an allosteric modulator. D. Suicide inactivators are examples of allosteric modulators.arrow_forward
- what is the first step in an enzyme-catalyzed reaction? a. formation of enzyme-substrate complex b. ionization of enzyme c. dimerizing the substance d. catalysis of enzymearrow_forwardWhat type of inhibition is observed from the shift of the Lineweaver-Burke plot ahown in the graph below where the solid Ine represents the uninhibited enzymatic reaction while the broken line represents the inhibited enzymatic reaction? A. Irreveraible inhíbítion B. Noncompetitive inhíbition C. Competitive inhíbition D. Uncompetitive inhibition Potassium cyanide ia a polson 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? A. Irreveraible inhibition c. Competitive inhibition D. Uncompetitive 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. Нуdrolase c. Isomerase D. Ligase Which of the following enzyme classes catalyze reactions in which two molecules become covalently linked to each other? A. Kinase B. Hydrolase…arrow_forwardWhich statement is true about noncompetitive inhibition? a. Binding of the inhibitor occurs to the active site of the enzyme b. Inhibition is irreversible c. Increasing the amount of substrate does not reverse the inhibition d. We talked about it in context of aspirin inhibiting blood clottingarrow_forward
- 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. antibioticarrow_forwardWhich of the following enzyme classes catalyze reactions in which two molecules become covalently linked to each other? A. Kinase B. Hydrolase C. Isomerase D. Ligasearrow_forwardHow does a non-competitive inhibitor decrease the rate of an enzyme reaction? O A. by binding at the active site of the enzyme B. by changing the shape of the active site on the enzyme, without binding to active site O C. by changing the free energy change of the reaction D. by acting as a coenzyme for the reactionarrow_forward
- What are allosteric modulators? A. These are inhibitors that bind at sites other than the active site of enzymes resulting in the reduction of enzyme activities B. These are activators that bind at sites other than the active sites of enzymes resulting in enhanced enzyme activities. C. These are either inhibitors or activators that bind at the active site of enzymes. D. These are either inhibitors or activators that bind at sites other than the active sites of enzymes reducing or enhancing the latter's activities. E. These are small molecules that bind to an ES complex only.arrow_forwardWhich of the following best explains why enzyme catalysis is affected by a change in pH? A. Change in pH alters ionization states of serine in the active site involved in nucleophilic catalysis B. The ionization states of his, asp and glu involved in acid/base catalysis are altered with change in pH C. Change in pH alters ionization states of contact amino acids in the active site D. All enzymes have optimum pHarrow_forwardThe important amino acid residues in the active site of enzyme X were found to be aspartic acid and lysine. In an experiment, the pH of the buffer solution in which enzyme X was dissolved was changed from pH 7 to pH 5. What would be the expected effect of this change on the enzyme’s catalytic activity? A. decrease B. increase C. unchanged D. cannot be determinedarrow_forward
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