Biological Science (7th Edition)
7th Edition
ISBN: 9780134678320
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Greg Podgorski, Emily Taylor, Jeff Carmichael
Publisher: PEARSON
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Textbook Question
Chapter 8, Problem 2TYK
What is a transition state?
a. the shape adopted by an enzyme that has an inhibitory molecule bound at its active site
b. the amount of kinetic energy required for a reaction to proceed
c. the intermediate complex formed as covalent bonds in the reactants are being broken and re-formed during a reaction
d. the structure of an enzyme when an allosteric regulatory molecule binds to it
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Students have asked these similar questions
If the environmental temperature gets too high, what will happen to an enzyme and the chemical reaction it catalyzes?
Group of answer choices
A. It will not encounter its substrates often, and the reaction will slow down.
B. It will crystallize, the active site will become inflexible and slow down the reaction.
C. It will denature, lose its shape, and the reaction will not occur.
D. It will become less fluid, and be unable to transport substances easily.
E. It will become more fluid, and speed up the reaction.
Match each reaction description to the type of enzyme that catalyzes the reaction.
1. Oxidation and reduction of compounds
2. Transfers a functional group from one compound to another compound
3. Utilizes water to break bonds within a compound
4. Addition/removal of a group of atoms and bonds within a compound
5. Forms a bond between two compounds
A. Ligase
B. Transferase
C. Hydrolase
D. Oxidoreductase
E. Isomerase
F. Lyase
A histidine was determined to be the critical residue involved in an enzyme-catalyzed reaction. If the pKa of the histidine is known to be 6.5 in the active site and the pH of maximum catalytic activity is 7.2, what is likely the primary role of histidine in the catalytic reaction?
A. forms a covalent bond with the substrate
B. reduces the entropy of the substrate
C. stabilizes a charged intermediate
D. acts as a proton donor
Aspartate and lysine are in the active site of an enzyme. They are both known to participate directly in catalysis. The pKa's of the residues are found to be 3.2 and 9.6, respectively for aspartate and lysine. The optimum pH for the enzyme is 6.4. Which forms of these two residues will predominate when the enzyme is most active?
A. aspartate is protonated; lysine is deprotonated
B. both residues are deprotonated
C. aspartate is deprotonated; lysine is protonated
D. both residues are protonated
Chapter 8 Solutions
Biological Science (7th Edition)
Ch. 8 - 2. What is a transition state?
a. the shape...Ch. 8 - 3. How does pH affect enzyme-catalyzed...Ch. 8 - Explain how feedback inhibition regulates...Ch. 8 - 5. Explain the lock-and-key model of enzyme...Ch. 8 - If you were to expose glucose to oxygen on your...Ch. 8 - Using what you have learned about changes in Gibbs...Ch. 8 - Prob. 10TYPSSCh. 8 - 15. The functional form of PAH contains four...
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- Which 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_forwardWhat are enzymes? A. Enzymes are biological catalysts made up of amino acids B. Enzymes are biological catalysts that create an environment to lower the energy expenditure to break "old" bonds. C. Enzymes are biological catalysts that provide a mechanism to make unfavorable reactions proceed. D. Enzymes are biological catalysts that require cofactors to effect catalysis E. Enzymes are biological catalysts that provide the means to channel chemical energy to allow biological transformations to occurarrow_forwardResearchers have identified an enzyme that can catalyze two different chemical reactions. Which of the following is most likely true based on this finding? A B C D The reactants involved in the two reactions are very similar in their charge and shape. The reactant in one reaction acts as an allosteric inhibitor while the reactant in the sec- ond acts as an allosteric activator. The enzyme contains both alpha-helices and beta-sheets in their secondary structures. The catalytic activity of the enzyme is dependent on both competitive inhibition and al- losteric regulation.arrow_forward
- Which statement defines a coenzyme? a. An enzyme precursor b. A unit consisting of an enzyme bound to reactants plus ATP c. An inactive enzyme that becomes functional upon contact with specific cofactors d. The active part of an enzyme e. An organic molecule closely associated with enzymesarrow_forwardWhich of the following is TRUE concerning the induced fit model of enzyme catalysis? * (One correct answer only) A. The active site can be influenced by molecules binding elsewhere on an enzyme B. The initial binding of enzyme and substrate is the most tightly bound conformation C. The induced fit must occur prior to the initial binding of enzyme and substrate in order for the reaction to proceed D. The binding of enzyme and substrate is weakest in the transition statearrow_forwardChoose 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_forward
- Which of the following statements are correct about how enzymes accelerate chemical reactions (select all that apply)? A. Enzymes bind substrates to raise their effective concentration B. Enzymes enhance the rate of a chemical reaction C. Enzymes catalyze chemical reactions by destabilizing transition states D. Side chains of protein provide reactive groups that facilitate reaction E. Enzymes shift the equilibrium of a chemical reaction to favor product formationarrow_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_forwardSuppose an enzyme and its substrate obey the lock and key model of enzyme catalysis. Which of the following would be true of the enzyme?Select all that apply A.the active site of the enzyme must be rigid B.the active site of the enzyme must be flexible C.only one substrate could be converted to product by the enzyme D.the enzyme could bind different substrates if the substrates shared a common motif somewhere in their structures E.the entire enzyme must be rigidarrow_forward
- Which one of the following statements is true of enzyme catalysts? a. Their catalytic activity is independent of pH. b. They are generally equally active on D and L isomers of a given substrate. c. They can increase the equilibrium constant for a given reaction by a thousand fold or more. d. They can increase the reaction rate for a given reaction by a thousand fold or more. e. To be effective, they must be present at the same concentration as their substrate.arrow_forwardWhich of the followingdescribe superior properties of enzymes (biological catalysts) over traditional chemical catalysts? a. They are mostly and generally operative under mild temperature, pressure, and pH conditions b. They are regulated only by substrate concentration c. They do not effect the reaction equilibrium, but lower the reaction's activation energy d. They are recycled at the end of the reaction Choose all that applyarrow_forwardWhich of the following describes a reaction that requires substrate 1 to bind the the enzyme, then substrate 2 binds, and then the products are produced? A. No ternary complex B. Ordered ternary complex C. Ping-Pong D. Random ternary complexarrow_forward
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