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 19TYK
Summary Introduction
Introduction: Enzyme is defined as a biological catalyst that speeds up the
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Enzymes play a fundamental role in cell function.
Regarding the biochemistry of enzymes, which of the following statements is correct?
A.
Enzymes increase the number of molecules that get to the transition state.
B.
Enzymes increase the rate of a spontaneous reaction by lowering the ΔG.
C.
Enzymes increase the enthalpy (H) of the products compared to the reactants.
D.
Most enzymes can bind and react with a wide range of different substrate molecules.
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.
Which of the following is a primary function of the active site of an enzyme?
a.
It binds allosteric regulators of the enzyme.
b.
It binds noncompetitive inhibitors of the enzyme.
c.
It catalyzes the reaction associated with the enzyme.
d.
It is activated by the presence of the end product of the metabolic pathway in which the enzyme is involved.
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Which of the following statement about the mass spectrometry is true?
a.
Large amount of protein sample is needed for mass spectrum, and thus it is very expensive.
b.
It is a powerful method to determine the 3-dimensional structure of proteins.
c.
It can be sued for protein location in a living cell.
d.
It can be used to measure the molecular weight of proteins.
e.
It can be used to determine the stability of a protein structure in solution.
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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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- Which statement about metabolic pathways is false? OA. A specific enzyme catalyzes each transformational step. B. Chemical transformations occur in a series of separate chemical reactions. O C. Inhibitors that target some key enzymes in a pathway can slow the rate of reaction. D. Activators that target some key enzymes in a pathway can increase the rate of reaction. E. In prokaryotes, reactions in a pathway are located in multiple compartments.arrow_forwardAccording to the lock-and-key model of enzyme action,a. reactants must first be heated.b. enzyme shape is not important.c. each enzyme can catalyze many types of reactions.d. reactants must bind to an active site on the enzyme.e. enzymes control only a small number of reactions in the cell.arrow_forwardPlease help with hw :} ATP is the energy currency of the cell.a. What about the structure of ATP makes it effective at storing free energy? b. Define what is meant by an endergonic or exergonic reaction. c. Explain how ATP can facilitate chemical reactions in the cell, using the terms endergonic and exergonic d. An enzyme is a biological catalyst. Explain what that means in terms of chemical reactions, including a discussion of transition states. e. Do enzymes affect the overall free energy change of a reaction? Explain.arrow_forward
- Examine which of the following statement are FALSE about enzymes. * (Please choose one correct answer) A. The enzyme specificity of binding depends on the precisely defined arrangement of atoms in an active site suggesting for the lock-and-key mechanism B. The enzyme in an enzyme catalyzed reaction increases the rate at which the substrate is converted into product while lowering energy of activation C. First order reaction means S < Km while when S > Km means its zero-order reaction D. Glucose oxidase catalyzes the oxidation of β-D-glucose but not α-D-glucose is an example of absolute specificity E. One of the enzymes involved in the transport of oxygen from the lungs to the capillaries of the tissue requires Fe+ for catalysis. Under conditions of iron deficiency wherein the enzyme my lack iron, the enzyme would be referred to as the holoenzyme.arrow_forwardWhich of the following statements about allosteric enzyme regulation are true. A. Allosteric regulation is always used to negatively regulate enzyme activity. B. Allosteric regulators are often end products of a biochemical pathway. C. Different allosteric regulators turn enzyme activity on or off by binding the same site. D. Binding of allosteric regulators alters the conformation of an enzyme.arrow_forwardWhich of the following statements regarding protein phosphorylation is FALSE? Select one: A. Phosphorylation is catalyzed by enzymes called protein kinases. B. Phosphorylation inhibits the activity of enzymes C. Aspartate residues can be phosphorylated. D. Phosphorylation is a reversible covalent modification of enzymes. Which is usually the slowest way to regulate a reaction in a metabolic pathway? Select one: A. Allosteric modulation B. Covalent modification C. Changing the enzyme concentration D. All of the above are usually equally as fastarrow_forward
- In biological systems, ATP functions bya. providing the energy to drive endergonic reactions.b. acting as an enzyme and lowering the activation energy of certainreactions.c. adjusting the pH of solutions to maintain optimal conditions forenzyme activity.d. regulating the speed at which endergonic reactions proceed.e. interacting with enzymes as a cofactor to stimulate chemical reactions.arrow_forwardWhich of the following is true for the induced-fit model of enzyme-substrate binding? A. The conformation of the enzyme’s active site changes when the enzyme binds to its substrate B. Stronger interactions between the enzyme and its substrate are formed as compared to the lock-and-key model of enzyme-substrate binding C. Both A and B D. Neither A nor B Which statement does not apply to transition states? A. only exist transiently (have lifetimes on the order of 10^-14 to 10^-13 seconds) B. differ in energy from the substrate by the activation energy C. Chemical bonds are in the process of being formed and broken. D. Many have been detected and purified experimentally.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
- 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…arrow_forwardSelect all the true statements about sequential versus concerted models of allostery. Group of answer choices 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_forwardnzymes play a fundamental role in cell function. Regarding the biochemistry of enzymes, which of the following statements is correct? A. Most enzymes can bind and react with a wide range of different substrate molecules. B. Enzymes increase the rate of a spontaneous reaction by lowering the ΔG. C. Enzymes increase the enthalpy (H) of the products compared to the reactants. D. Enzymes increase the number of molecules that get to the transition state.arrow_forward
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