EP CONNECT ONLINE ACCESS FOR BIOLOGY
20th Edition
ISBN: 9781260494655
Author: Raven
Publisher: MCG COURSE
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Textbook Question
Chapter 6, Problem 5A
Enzymes have similar responses to both changes in temperature and pH. The effect of both is on the
a. rate of movement of the substrate molecules.
b. strength of the
c. three-dimensional shape of the enzyme.
d. rate of movement of the enzyme.
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Students have asked these similar questions
The enzyme activity is:
A. to The number of grams of substrate that react to form product, per mole of enzyme, per unit of time.
b. The number of moles of substrate that react to form product, per gram of enzyme, per unit time.
c. The number of moles of substrate that react to form product, per mole of enzyme, per unit time
d. The number of grams of substrate that react to form product, per gram of enzyme, per unit of time.
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…
Which of the following statements about Competitive and noncompetitive inhibition is false?
a. A noncompetitive inhibitor does not change the Km of the enzyme.
b. A competitive inhibitor does not change the Vmax of the enzyme
c. The noncompetitive inhibitor can bind either free enzyme or the enzyme–substrate complex.
d.A competitive inhibitor decreases the apparent Km for a given substrate.
Chapter 6 Solutions
EP CONNECT ONLINE ACCESS FOR BIOLOGY
Ch. 6.1 - Prob. 1LOCh. 6.1 - Prob. 2LOCh. 6.1 - Describe the nature of redox reactions.Ch. 6.2 - Explain the laws of thermodynamics.Ch. 6.2 - Prob. 2LOCh. 6.2 - Contrast the course of a reaction with and without...Ch. 6.3 - Describe the role of ATP in short-term energy...Ch. 6.3 - Prob. 2LOCh. 6.4 - Discuss the specificity of enzymes.Ch. 6.4 - Explain how enzymes bind to their substrates.
Ch. 6.4 - Prob. 3LOCh. 6.5 - Prob. 1LOCh. 6.5 - Prob. 2LOCh. 6.5 - Prob. 3LOCh. 6 - Prob. 1DACh. 6 - A covalent bond between two atoms represents what...Ch. 6 - During a redox reaction the molecule that gains an...Ch. 6 - Prob. 3UCh. 6 - A spontaneous reaction is one in which a. the...Ch. 6 - Prob. 5UCh. 6 - Which of the following is NOT a properly of a...Ch. 6 - Where is the energy stored in a molecule of ATP?...Ch. 6 - Prob. 1ACh. 6 - Which of the following statements is NOT true...Ch. 6 - Prob. 3ACh. 6 - Prob. 4ACh. 6 - Enzymes have similar responses to both changes in...Ch. 6 - Prob. 6ACh. 6 - Examine the graph showing the rate of reaction...Ch. 6 - Phosphofructokinase functions to add a phosphate...
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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
- 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_forwardThe 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_forwardMatch the following terms with the best definition. Enzyme Product Substrate Active Site A. A macromolecule serving as a catalyst. B. A material resulting from a chemical reaction. C. The reactant on which an enzyme works. D. Location on an enzyme where the reaction is catalyzed.arrow_forward
- When measuring reaction velocity as a function of substrate concentration, a researcher usually keeps the concentration of enzyme at a constant level. What would happen if the enzyme concentration were not kept constant? A. Vmax would change, but Km would remain constant. B. Both Vmax and Km would change C. Vmax would remain constant, but Km would change D. Vmax would remain constant, but V would change E. None of the above would necessarily occurarrow_forwardIn competitive inhibition, increasing concentrations of the inhibitor will have the following effect on the kinetics of the enzyme: A. Km will decrease. B. Vmax will stay the same. C. The reaction will cease because the inhibitor binds irreversibly. D. Km / Vmax will stay the same.arrow_forwardA noncompetitive inhibitor (Circle one). a. Binds at the active site of the enzyme. b. Alters the three-dimensional structure of the enzyme. c. Increases the rate of the enzyme-catalyzed reaction. d. Has a structure similar to the substrate. e. Has its effect reversed by adding more substrate.arrow_forward
- Which 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 ONE of the following would be most effective as a feedback mechanism for anenzymatic reaction? A. Reduced concentration of the product B. A change in pH C. Increased concentration of substrate D. Temporary binding of a non-substrate molecule in the active binding sitearrow_forwardAll of the following increase enzymatic activity except a. an increase in temperature. b. an increase in pH. c. an increase in concentration of the substrate. d. an increase in concentration of the enzyme that catalyzes the reaction.arrow_forward
- Please choose one of these answers A. An allosteric inhibitor appeared B. There was a dramatic change jn the pH. C. The enzyme had achieved its maximum velocity. D. The enzyme had denatured E. A large amount of the substrate had been consumed.arrow_forwardSome enzymes function to breakdown harmful compounds that if allowed to accumulate could cause death. Below is a plot of the velocity of enzyme catalysis as a function of substrate concentration. Which one of the curves shown here is most likely for an enzyme that catalyses the breakdown of a toxic compound? A. A B. B C. C D. Darrow_forwardAn enzyme has the ability to catalyze reactions of several unrelated compounds. The mechanism of how this enzyme operates is best explained by a. the lock-and-key theory b. the induced-fit theory c. the enzyme-substrate complex d. the efficiency of the enzymearrow_forward
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