Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN: 9781305389892
Author: Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher: Cengage Learning
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Textbook Question
Chapter 6, Problem 6TYK
Which of the following methods is not used by enzymes to increase the
a. covalent bonding with the substrate at their active site
b. bringing reacting molecules into close prosimity
c. orienting reactants into positions to favor transition states
d. changing charges on reactants to hasten their reactivity
e. increasing fit of enzyme and substrate that reduces the energy of activation
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Students have asked these similar questions
Which of the following is incorrect?
a. Without an enzyme, reaction rate can be increased by increasing the [reactants]
b. Enzymes increase reaction rate by bringing the substrates to close proximity
A conformational change in an enzyme upon binding of a substrate is called "induced fit"
Od. None; all the other choices are correct
OC.
Which of the following statements is false?
a. A reaction may not occur at a detectable rate even though it has a favorable equilibrium.
b. After a reaction, the enzyme involved becomes available to catalyze the reaction again.
c. For S → P, a catalyst shifts the reaction equilibrium to the right.
d. Lowering the temperature of a reaction will lower the reaction rate.
e. Substrate binds to an enzyme's active site.
INSTRUCTIONS
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Chapter 6 Solutions
Biology: The Dynamic Science (MindTap Course List)
Ch. 6.1 - Prob. 1SBCh. 6.1 - In thermodynamics, what is meant by an isolated...Ch. 6.2 - Prob. 1SBCh. 6.2 - Prob. 2SBCh. 6.2 - Distinguish between exergonic and endergonic...Ch. 6.3 - Prob. 1SBCh. 6.3 - How are coupled reactions important to cell...Ch. 6.4 - How do enzymes increase the rates of the reaction...Ch. 6.4 - Can enzymes alter the G of a reaction?Ch. 6.5 - Prob. 1SB
Ch. 6.5 - What is the difference between competitive and...Ch. 6.5 - Prob. 3SBCh. 6.6 - Prob. 1SBCh. 6 - The capacity to do work best defines: a metabolic...Ch. 6 - The assembly of proteins from amino acids is best...Ch. 6 - When two glucose molecules react to form maltose:...Ch. 6 - When glucose reacts with ATP to form...Ch. 6 - In the following graph: A represents the product....Ch. 6 - Which of the following methods is not used by...Ch. 6 - In an enzymatic reaction: a. the enzyme leaves the...Ch. 6 - Which of the following statements about the...Ch. 6 - Which of the following statements about inhibition...Ch. 6 - Which of the following statements is incorrect? a....Ch. 6 - Prob. 11TYKCh. 6 - Discuss Concepts Trace the flow of energy through...Ch. 6 - Prob. 13TYKCh. 6 - Prob. 14TYKCh. 6 - Prob. 15TYKCh. 6 - Prob. 16TYKCh. 6 - Prob. 17TYKCh. 6 - Prob. 1ITDCh. 6 - Prob. 2ITDCh. 6 - Prob. 3ITD
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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
- 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.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_forwardWhich of the following is NOT true about enzymes A. they do not alter reaction equilibria B. they accelerate the forward rate of a reaction C. they decrease ∆G’0 of a reaction D. they accelerate the reverse rate of a reaction E. they stabilize transition statesarrow_forward
- An 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_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_forwardWhich of the following statements is not true about enzymes?* A. Enzymes are biological catalysts B. Enzymes as catalysts lowers the activation energy thus, speeds up the rate of reaction C. Enzymes are proteins D. Enzymes are highly specific E. None of the given optionsarrow_forward
- Choose the wrong statement: Select one: O a. Competitive inhibitors competing with the substrate O b. Each enzyme has active and inactive forms c. exergonic reaction release of free energy O d. Cofactors are protein- organic enzyme helpersarrow_forwardWhich of the following is TRUE about the enzymatic catalysis of a chemical reaction? A. It increases the energy of the transition state B. It decreases the free energy ∆G so that a reaction can proceed spontaneously C. It decreases the energy of the transition state D. It increases the forward and reverse ratesarrow_forwardEnzymes work by at least three mechanisms. Which of the following is NOT a mechanism by which enzymes function? A. by putting reactants in close proximity to each other. B. by altering the free energy ( ΔG) of the reaction. C. by orienting the reactants so they are positioned to favour the transition state. D. by altering the immediate environment of the reactants to promote reactant interactions.arrow_forward
- Which 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_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_forwardYou are studying the enzyme Homerase and you notice that the rate of product formation increases as you add more substrate to a constant number of enzymes. However past a certain concentration of added substrate molecules, the rate no longer increases even though you keep increasing the substrate concentration. Which of the following statements likely accounts for this observation? a. This is an example of feedback inhibition b. Since the free energy for the reaction doesn't change in the presence of an enzyme, it can only reach a certain energy level maximum c. The product molecules must be acting as competitive inhibitors d. All the enzymes are complexed with substrate moleculesarrow_forward
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