Biology (MindTap Course List)
11th Edition
ISBN: 9781337392938
Author: Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 7, Problem 8TYU
Test Your Understanding
8. “Induced fit” means that when a substrate binds to an enzyme’s active site, (a) it fits perfectly, like a key in a lock (b) the substrate and enzyme undergo conformational changes (c) a site other than the active site undergoes a conformational change (d) the substrate and the enzyme become irreversibly bound to each other (e) c and d
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
“Induced fit” means that when a substrate binds to an enzyme’s active site, (a) it fits perfectly, like a key in a lock (b) the substrate and enzyme undergo conformational changes (c) a site other than the active site undergoes aconformational change (d) the substrate and the enzyme become irreversibly bound to each other (e) c and d
(a) Induced fit
(b) Active site
(c) Transition state
(d) AG"
(e) Coenzymes
(f) Holoenzyme
(g) Apoenzyme
(h) Cofactor
(i) Substrate
(j) Enzyme
Suicide Inhibitor
Oxyanion hole
Catalytic triad
Alkoxide ion
Specificity pocket
Protease
Competitive inhibitor
Uncompetitive inhibitor
Noncompetitive inhibitor
Siamese Cats
1. Enzyme minus its cofactor
2. Reactant in an enzyme-catalyzed reaction
3. A coenzyme or metal
4. The least stable reaction intermediate
5. Protein catalyst
6. Site where enzyme catalysis takes place
7. Function of K'eq
8. Change in enzyme structure
9. Enzyme plus cofactor
10. Small vitamin-derived organic cofactors
(1) Tryptophan, Tyrosine, Phenylalanine
(2) Inhibitor and substrate bind simultaneousl
(3) Tyrosinase
(4) Potent nucleophile
(5) Binds enzyme/substrate complex only
(6) Irreversible
(7) Active site
(8) Inhibitor binds active site
(9) Stabilizes tetrahedral intermediate
(10) Hydrolysis
8). Which statement best describes
1 point
the enzyme represented in the
graphs?
O 10 20 30 40 50 60
O 2 4 6
10 12
Temperature ("C)
PH
(1) This enzyme works best at a
temperature of 50°C and a pH of 12.
(2) Temperature and pH have no effect on
the action of this enzyme.
(3) This enzyme works best at a
temperature above 50°C and a pH above 12.
(4) This enzyme works best at a
temperature of 35°C and a pH of 8.
Relative Rate of
Enzyme Action
Relative Rate of
Enzyme Action
Chapter 7 Solutions
Biology (MindTap Course List)
Ch. 7.1 - Define energy, emphasizing how it is related to...Ch. 7.1 - Use examples to contrast potential energy and...Ch. 7.1 - Prob. 1CCh. 7.2 - Prob. 3LOCh. 7.2 - Prob. 1CCh. 7.2 - Life is sometimes described as a constant struggle...Ch. 7.3 - Prob. 4LOCh. 7.3 - Prob. 5LOCh. 7.3 - Prob. 6LOCh. 7.3 - Prob. 1C
Ch. 7.3 - Prob. 2CCh. 7.4 - Explain how the chemical structure of ATP allows...Ch. 7.4 - Prob. 1CCh. 7.4 - Prob. 2CCh. 7.5 - Relate the transfer of electrons (or hydrogen...Ch. 7.5 - PREDICT Which has the most energy, the oxidized...Ch. 7.6 - Explain how an enzyme lowers the required energy...Ch. 7.6 - Describe specific ways enzymes are regulated.Ch. 7.6 - Prob. 1CCh. 7.6 - How does the function of the active site of an...Ch. 7.6 - How are temperature and pH optima of an enzyme...Ch. 7.6 - Prob. 4CCh. 7 - Which of the following can do work in a cell? (a)...Ch. 7 - Prob. 2TYUCh. 7 - Prob. 3TYUCh. 7 - Test Your Understanding 4. Diffusion is an (a)...Ch. 7 - Prob. 5TYUCh. 7 - Prob. 6TYUCh. 7 - Prob. 7TYUCh. 7 - Test Your Understanding 8. Induced fit means that...Ch. 7 - Prob. 9TYUCh. 7 - Prob. 10TYUCh. 7 - PREDICT In the following reaction series, which...Ch. 7 - Test Your Understanding 12. EVOLUTION link All...Ch. 7 - EVOLUTION LINK Some have argued that evolution is...Ch. 7 - Prob. 14TYUCh. 7 - Prob. 15TYUCh. 7 - Prob. 16TYU
Knowledge Booster
Learn more about
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
- C)|Myth: The specificity of an enzyme for its substrate is explained by the lock and key hypothesis. Fact: The lock and key hypothesis is outdated! What is our current model for understanding regarding how enzymes recognize and bind to substrates?arrow_forwardPractice Mira Gendy 1 of 1 Directions: This short free-response question requires about 6 minutes to answer. The question is worth 3 points. Read the question carefully and completely. Answers must be written out in paragraph form. Outlines, bulleted lists, or diagrams alone are not acceptable. II Substrate Concentration [S] The graph above shows the initial rate of an enzyme-catalyzed reaction at different substrate concentrations in the presence of a constant concentration of the enzyme. Connect the primary structure of the enzyme to its overall shape. I U x X2 5 Initial Rate of Reactionarrow_forwardExplain how the following mechanisms regulate enzyme activity.(a) Covalent modification (b) Genetic control(c) Allosteric regulation (d) Feedback inhibitionarrow_forward
- 2. The kinetic effect of purely competitive inhibitor of an enzyme: (A) Increases K without affecting Vmax (B) Decreases Km without affecting Vmax (C) Increases Vmax Without affecting K (D) Decreases Vmax without affecting Km 3. In reversible non-competitive enzyme activity inhibition: (A) Vma is increased (C) Vmax is decreased 4. In enzyme kinetics Vmax reflects: (A) The amount of an active enzyme (C) Half the substrate concentration 5. In non-competitive enzyme activity inhibition, inhibitor: (A) Increases Km (C) Does not affect Km (B) K is increased (D) Concentration of active enzyme is reduced (B) Substrate concentration (D) Enzyme substrate complex (B) Decreases Km (D) Increases Kmarrow_forward2. Enzyme-catalyzed reactions. Answer the following with true or false. If false, explain why. (a) The initial rate of an enzyme-catalyzed reaction is independent of substrate concentration. (b) At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. (c) The Michaelis constant Km equals the substrate concentration at which velocity (v) = Vmax/2. (d) The Km for a regulatory enzyme varies with enzyme concentration. (e) If enough substrate is added, the normal Vmax of an enzyme-catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. (f) The Km of some enzymes may be altered by the presence of metabolites structurally unrelated to the substrate. (g) The rate of an enzyme-catalyzed reaction in the presence of a rate-limiting concentration of substrate decreases with time. (h) The sigmoidal shape of the v versus [S] curve for some regulatory enzymes indicates that affinity of the enzyme for the…arrow_forward5. By using Excel or GoogleSheets. graph the Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and Kwax values for the inhibited and uninhibited reactions? Is the inhibitor competitive or noncompetitive? [S] (mM) V, No Inhibitor (mmol min-) V, Inhibitor Present (mmol min-') 1 × 10-4 5 × 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 0.026 0.010 0.092 0.136 0.040 0.086 0.150 0.120 0.165 0.142arrow_forward
- 5. Enzymes are incredibly effective at facilitating chemical reactions and must be controlled- or the chemical reaction won't stop and the reactant(s) might be used up. (A) Use 3 different colors to color the coding circles and corresponding structures in the figures. (B) Draw an arrow pointing to the active site in each figure. (C) Beneath each diagram, write the type of inhibition and briefly, in your own words, explain what is happening. PG al JartW Mool bluow nolsoeen er edw gni nobisvitae ert wori gniworla en qsp/ru to can't S uid can't weib (A) wole Ts w.bind b (8) bris bobl ewm bind oll omysne erlf yd beoue o.gons O Enzyme O Reactant (substrate) O Inhibitor Enzyme Enzyme Type of inhibition: Type of inhibition:arrow_forwardENZYME CATALYSIS lab Construct a hypothesis addressing the effect concentration will have on rate of reaction. What chemical reaction is being catalyzed in the experiment? Label the substrate(s), enzyme and product(s).arrow_forwardA) Myth: Enzymes are specific for one substrate. Fact: Like most enzymes, alliinase can act on multiple different substrates. Explain why most enzymes can act on more than one substrate compound. (Refer to the “Alliin-like Substrates" panel in your answer.)arrow_forward
- A. 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_forwardIn vitro conditions the enzyme is used in catalytic amounts (10-12 to 10-8M). Estimate the amount of enzyme in living cell. Assuming (a) fresh tissue is 80% water and intracellular (b) total soluble protein in cell represents 15% of wet weight (c) all soluble proteins are enzymes (d) average molecular weight of protein is 150,000 (e) about 1000 different enzymes are present.arrow_forward(a) Lock and key model versus induced fit model of enzyme activity. (b) Competitive and non-competitive enzyme inhibitors. (c) Reversible and irreversible enzyme inhibitors. Answer Allarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Biology (MindTap Course List)BiologyISBN:9781337392938Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. BergPublisher:Cengage Learning
Biology: The Dynamic Science (MindTap Course List)BiologyISBN:9781305389892Author:Peter J. Russell, Paul E. Hertz, Beverly McMillanPublisher:Cengage Learning
Biology (MindTap Course List)
Biology
ISBN:9781337392938
Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher:Cengage Learning
Biology: The Dynamic Science (MindTap Course List)
Biology
ISBN:9781305389892
Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher:Cengage Learning
Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License