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 11TYU
PREDICT In the following reaction series, which enzyme(s) is/are most likely to have an allosteric site to which the end product E binds? (a) enzyme 1 (b) enzyme 2 (c) enzyme 3 (d) enzyme 4 (e) enzymes 3 and 4
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When biological enzymes are heated, they lose their catalytic activity. The change that occurs is an ENDOTHERMIC and SPONTANEOUS process.
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Based on the given information, what is the sign of Δ˚H?
Is the structure of the original enzyme MORE or LESS ordered than the new form? Explain your answer.
Which of the following would best explain how an enzyme catalyzes two different reactions?
A) The enzyme contains a-helices and B-pleated sheets.
B) The enzyme is subject to cooperativity
C) Either the enzyme has two distinct active sites or the substrates involved in the two reactions have very similar structures
D) The enzyme is subject to competitive inhibition and allosteric regulation
E) The enzyme is composed of at least two subunits
You make a fresh fruit salad. To prevent them from turning brown, due to a reaction of the enzyme phenolase present in apples and bananas, you add lemon juice and place the fruit salad in the refrigerator at 4o C. Explain these two actions. In your explanation, specify the mechanism of action involved.
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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- The enzyme E catalyzes the chemical reaction, X ⇌ Y. Imagine two different cases, a) initial concentration of X is low, and b) initial concentration of X is high. Now, if you start adding X, the initial velocity will increase until it reaches its maximum level. In which case, the initial velocity will increase linearly with an increase in the concentration of X? why?arrow_forwardWhich of the following statements helps best explain the reaction specificity of an enzyme? a) The shape and charge of the substrates are compatible with the active site of the enzyme. b) The free energy of the reactants is greater than the free energy of the products. c) The equilibrium constant of the reaction is much greater than 1. d) The concentration of the enzyme inside living cells is greater than the concentration of substrate.arrow_forwardWhich 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_forward
- Consider the analogy of the jiggling box containing coins that was described on page 85. The reaction, the flipping of coins that either face heads up (h) or tails up (T), is described by the equation h ↔ T, where the rate of the forward reaction equals the rate of the reverse reaction.a. What are ΔG and ΔG° in this analogy? b. What corresponds to the temperature at which the reaction proceeds? What corresponds to the activation energy of the reaction? assume you have an “enzyme,” called jigglase, which catalyzes this reaction. What would the effect of jigglase be and what, mechanically, might jigglase do in this analogy?arrow_forwardThe following reaction coordinate diagram charts the energy of a substrate molecule (S) as it passes through a transition state (X‡) on its way to becoming a stable product (P) alone or in the presence of one of two different enzymes (E1 and E2). How does the addition of either enzyme affect the change in Gibbs free energy (ΔG) for the reaction? Which of the two enzymes binds with greater affinity to the substrate? Which enzyme better stabilizes the transition state? Which enzyme functions as a better catalyst?arrow_forwardYou have been the only one who has been able to this. It has three other parts as well, A) Which Enzyme Catalyzes this reaction? choices are in image provided. B) What is ∆G°' for this reaction? Answer in Joules. K' = 19 C) If the concentration of Glucose-1-phosphate is 48.82 µM at equilibrium, what is the concentration of Glucose-6-phosphate in µM? D) If the reaction is not at equilibrium, what is ∆G' at 25°C if the concentration of Glucose-1-phosphate is 15.04µM and the concentration of Glucose-6-phosphate is 1.62 mM? Answer in Joules. Pay attention to units. Round to the correct number of significant figures. There are 103 µM in 1mM. Thank you and you are the winner for Genius of the day!!arrow_forward
- “Enzyme increases the rate of a reaction by lowering the activation energy. In doing so, it also changes the equilibrium of that reaction.” Do you agree/disagree with this statement? And why?arrow_forwardConsider an enzyme catalyzed reaction taking place in an aqueous solution. If the earlier process of folding the enzyme results in a large decrease in the entropy of the system, how would this impact the rate of the catalyzed reaction.arrow_forwardCalculate the factor by which the enzyme will decrease the rate of the reaction with the following information. ES complex releases 30kj/mol of binding free energy that lowers the activaiton energy barrier needed for the transition state.arrow_forward
- A 63-year-old-man is discovered to have high levels of cholesterol in his blood during a routine check-up. He is prescribed atorvastatin, a drug that acts as an inhibitor of an enzyme involved in cholesterol synthesis. What is an enzyme? Describe Michaelis-Menten enzyme kinetics and discuss the effects of different kinds of enzyme inhibitors.arrow_forwardThe graph presented here depicts the activation energy, or the amount of energy needed for a reaction to proceed, with and without an enzyme. a. Which reaction requires more energy to proceed—the one with or without an enzyme? How do you know? b. Is this reaction anabolic or catabolic? How do you know?arrow_forwardSome cool enzyme (CE) catalyzes the conversion of compound F to compound A. Which of the following must be true of CE? Choice 1 of 4: CE can facilitate conversion of compound A into compound F. Choice 2 of 4: CE binds more tightly to the substrate F than to the product A. Choice 3 of 4: CE decreases the energy of the transition state between compounds F and A. Choice 4 of 4: CE facilitates net conversion of F to A whenever F is present.arrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License