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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Textbook Question
Chapter 8, Problem 10TYK
What is meant by an induced fit?
- a. The binding of the substrate is an energy-requiring process.
- b. A competitive inhibitor can outcompete the substrate for the active site.
- c. The binding of the substrate changes the shape of the active site, which can stress or bend substrate bonds.
- d. The binding of an activator to an allosteric site induces a more active form of the subunits of an enzyme.
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Students have asked these similar questions
The concept of “induced fit” refers to the fact that:
a. enzyme specificity is induced by enzyme-substrate binding.
b. enzyme-substrate binding induces an increase in the reaction entropy, thereby catalyzing the reaction.
c. enzyme-substrate binding induces movement along the reaction coordinate to the transition state.
d. substrate binding may induce a conformational change in the enzyme, which then brings catalytic groups into proper orientation.
e. when a substrate binds to an enzyme, the enzyme induces a loss of water (desolvation) from the substrate.
The active site of an enzyme binds specifically to a substrate. Your text mentions an early idea which is that this enzyme-to-substrate interaction is like a lock and key, but it then describes a more accurate model for how enzymes bind to their substrates. Explain why the interaction is not like a lock and key and more like a hand grasping a doorknob. What is the specific name of the 'model' of how enzymes bind to their substrates?
Choose only the letter, no explanation needed.
Enzyme activity is affected by a variety of factors. What factor causes the enzyme to denature if it becomes extremely high? *
Choices:
A. Water's Effect
B. pH
C. Temperature
D. Activator's Effect
An inhibitor binds to the enzyme's active site, preventing the substrate from binding to it. What conclusions can you make from this situation? *
A. No reaction occurred
B. Non-competitive inhibition occurred
C. Enzyme activity occurred
D. Competitive inhibition occurred
Each enzyme is very selective when it comes to its substrate. What can you conclude from this statement? *
A. Any substrate can bind to the active site.
B. Enzymes are used up in the reaction.
C. Only a specific substrate can bind to the active site.
D. Enzymes break down when not used.
Lock : Key :: Active Site : _____________________________ *
A. Substrate
B. Active Site
C. Coenzyme
D. Cofactor
Enzymes only speed up biological functions, so they are NOT used up in the…
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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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Evaluate the following statements concerning enzyme kinetics. Which one of the statements is false? a. Enzyme saturation fluctuates. b. In an uninhibited enzymatic reaction system, adding an excess of substrate will increase the reaction velocity beyond Vmax. c. The Vmax of an enzyme kinetics graph represents the point at which the enzyme is saturated with substrate. d. Non-competitive inhibition of an enzymatic reaction can be overcome by adding more unaltered enzyme. e. The activation energy of a reaction can be reduced by the presence of an enzyme.arrow_forwardHow can a noncompetitive inhibitor affect enzymeactivity without binding to the active site?a. It binds to another location on the enzyme, altering the active site shape.b. It physically blocks the entrance to the active site.c. It alters the shape of the substrate, making it difficult for it to bind to theactive site.d. It degrades the substrate.arrow_forwardFoF1 ATPase is the enzyme that catalyzes ATP synthesis. The enzyme itself is deactivated by ATP. What mode of enzyme regulation is being exemplified? Select the correct response: Trasncriptional control Covalent modification Proteolytic modification Allosteric regulation Compartmentationarrow_forward
- You have isolated a dimeric enzyme that contains two identical active sites. The binding of substrate to one active site decreases the substrate affinity of the other active site. Can the concerted model account for this negative cooperativity?arrow_forwardWhich statement is/are TRUE about inhibitors? A. Mode of action of penicillin on bacteria is an example of irreversible inhibition. B. Increasing the substrate concentration does not affect competitive inhibitors C. Uncompetitive inhibitors bind only to the enzyme-substrate complex D. In the Lineweaver-Burke plot, the lines for enzymes in the presence and absence of noncompetitive inhibitor have different x-intercepts.arrow_forwardA. Which enzyme model involves the enzyme staying the same shape when the substrate binds to it? (lock and key, induced fit) B. If an inhibitor has similiar structure to that of a substrate, does it act as a competitive or noncompetitive inhibitor? C. What is the surface for an active site for an ezyme that binds the substrate to that site?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_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_forwardcompare the state of an enzyme active site at a low substrate concentration and at a high substrate concentration. How does this affect the rate of the reaction?arrow_forward
- Select all the true statements about sequential versus concerted models of allostery. a. In sequential allostery, binding of the substrate on one end of an enzyme causes a conformational change on the other end which propagates to another enzyme and enables easier binding of a second substrate to the second enzyme b. No conformational changes occur in either model c. In concerted allostery, the two forms of the enzyme exist in equilibrium because of a conformational change independent of substrate binding d. In concerted allostery, binding of the substrate to one of the forms is favorable (but not to the other) and binding of the second substrate is enhanced on the favorable formarrow_forwardWhich of the following does NOT describe enzyme-catalyzed rate acceleration derived from the binding of substrate to enzyme a. repulsion between like charges b. substrate proximity and orientation c. reduction of entropy (increased order) d. desolvation of the substrate by the enzyme active site e. introduction of strain in bonds that need to breakarrow_forwardMany pharmaceuticals exert their action by inhibiting the activity of enzymes. Choose the false statement regarding enzyme inhibition. A- Enzyme can be inhibited by a ligand that binds to an active site B- Enzyme can be inhibited by a ligand that binds to a site other than that of substrate C- Enzyme can be inhibited by a ligand that forms a covalent bond with enzyme. D- It is true of all enzyme inhibitors, that the degree of inhibition is reduced when the concentration of inhibitor is lowered by metabolism or E- Enzyme may be inhibited by a ligand that does not bind in the substrate sitearrow_forward
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