Biology (MindTap Course List)
11th Edition
ISBN: 9781337392938
Author: Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher: Cengage Learning
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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
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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
Solve it and give reason for your answer
(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
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
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- 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 Actionarrow_forwardC)|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_forwardNeed explanation in detailsarrow_forward
- Practice 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_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
- 9arrow_forward5. 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_forward5 Kinetic data was collected for a new enzyme and its substrate. The same data has been plotted in two ways, v vs. [S] and 1/v vs. 1/[S]. Use these plots to answer the following questions about its enzymatic properties. 6 v(micromole/sec) 4 1/v (sec/micromole) 2.4 2.2 2 1.8 1.6 1.4 1.2 1 0.8 0.6 0.4 0.2 0 0 50 100 150 [S] (MM) 200 250 300 -0.3 -0.2-0.1 0 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1 1/[S] (1/mM) a. b. Determine Vmax and Kм for enzyme and its substrate. Don't forget to justify your work and include units! Vmax 5 umol/sec Km = 10 mM You duplicated the above experiment, but this time at a higher initial enzyme concentration. Draw on BOTH of the plots above what you expect the new data will look like at the higher enzyme concentration. Explain how this affects your Vmax and KM values, if at all. Vmax increases, Km stays the same as you increase enzyme concentrationarrow_forward
- Temperature and enzymatic activity Grade 9 students posed the following question: "What is the convenient temperature for the activity of an enzyme?" For this reason, they realized the experiment described below: -They put the same quantity of cooked starch in each of the two test tubes A and B. -They added a small quantity of fresh saliva to each of the two tubes. -Then, they placed both tubes for a convenient duration at different temperatures: •Tube A in ice where the temperature is 0°C Tube B in a water bath where the temperature is 37°C. N.B.: Saliva contains an enzyme: amylase. •The chemical medium is neutral in both tubes A and B. By using an appropriate technique, these students obtained the results shown in the opposite document. 1- Represent, in the same table, the variation of the quantities of cooked starch in the tubes A and B in function of time. 2- Pick out the posed problem by grade 9 students. 3- Analyze the obtained results. What do you conclude? Quantity of cooked…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_forward1 The Asp residue with a pka = 6 is found in the active site of an enzyme. This residue acts as an acid catalyst. Assuming that the enzyme is stable at a wide range of PH and that the Aspartic acid residue is the only ionizable residue in the active site, please draw the curve of enzyme activity versus pH on the graph below and explain the shape of your curve. (10 points) 100 % enzyme activity 75 50 25 3 LO 5 7 pH T 9 11arrow_forward
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