Biology (MindTap Course List)
10th Edition
ISBN: 9781285423586
Author: Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher: Cengage Learning
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Chapter 7, Problem 7TYU
Summary Introduction
Introduction: Enzymes are biological protein catalysts that alter the speed of a reaction in the biological system. The
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Explain how the following mechanisms regulate enzyme activity.(a) Covalent modification (b) Genetic control(c) Allosteric regulation (d) Feedback inhibition
Assume that an inhibitor (I) can bind to an enzyme and is modified by the enzyme. The modified inhibitor (I*) is then permanently associated with the active site of the enzyme, thus inhibiting the enzyme activity. Such inhibitors are called:
Suicide substrates
Transition-state analogs
Both A and B
Neither A nor Bwhich answer choice is correct im confused... thx
“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
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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- (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_forwardExamine the figure below, which compares the energetics of a catalyzed and uncatalyzed reaction during the progress of the reaction from substrate (S) to product (P). The highest peak in such a diagram corresponds to the transition state, which is an unstable, high-energy arrangement of substrate atoms that is intermediate between substrate and product. The free energy required to surmount this barrier to the reaction is termed the activation energy. Enzymes function by lowering the activation energy, thereby allowing a more rapid approach to equilibrium. UNCATALYZED activation energy progress of reaction CATALYZED activation energy S ES | progress of reaction free energy free energyarrow_forwardA substrate is converted to a product via the reaction sequence (1) E +S ES k2 (2) ES + S ES2 k4 (3) ES2 ES +P (4) ES , E +P (a). Using pseudo-steady state hypothesis for various forms of enzyme active sites, obtain relations between rates of individual steps in the mechanism. (b). Relating concentrations of vacant active sites to concentrations of occupied active sites, obtain expressions for the rate of consumption of S, (-Rs), and the rate of formation of P, Rp. (c). What are the maximum values of (-Rs) and Rp and under which conditions are these attained?arrow_forward
- Which of the two graphs, below, represents an enzyme catalyzed version of the reaction Y-->X? Utilizing your understanding of enzyme function, clearly explain why you chose your answer. activation energy for reaction Y-X activation energy for reaction Y X reactant reactant product product (A) uncatalyzed reaction pathway enzyme-catalyzed reaction pathway (8) total energy- total energyarrow_forwardFill in blanks with increased decreases or levels offarrow_forwardFor an enzyme that obeys Michaelis-Menten kinetics, in order for the reaction velocity (v) to be 80% of the maximal velocity (Vmax), the substrate concentration must be…. Choice 1 of 5:½ Km Choice 2 of 5:2 Km Choice 3 of 5:4 Km Choice 4 of 5:8 Km Choice 5 of 5:not enough information is givenarrow_forward
- a) What is the Steady State assumption; how does steady state differ from equilibrium? b) Transition state; what are two ways that enzymes can decrease the transition state energy?arrow_forwardThe reaction pathway labeled (A) below represents a substrate (protein) and a specific coenzyme (ATP). Reactions such as that found in (A) are catalyzed by enzymes called ATP (P ADP A Protein Proteinarrow_forwardIndicate whether each of the following statements about an enzyme active site is true or false. a. It is the location where substrate molecules are produced. b. It always has a fixed, rigid geometry. c. It always has a geometrical shape exactly complementary to that of substrate. d. It always accomodates several structurally related substrates. e. It is the location where substrate molecules are converted to product molecules. f. It always has a shape that has a degree of flexibility to it. g. it always accomodates only one specific substrate.arrow_forward
- Which type of enzyme regulation is best for the following situations?(a) An enzyme that becomes overactive during a disease(b) An enzyme needed only when there is low blood glucose(c) An enzyme that springs into action when a traumatic injury occurs(d) An enzyme needed only during adolescencearrow_forwardEnzyme X and enzyme Y catalyze the same reaction and exhibit the νo versus [S] curves shown below. Which enzyme is more effi cient at low [S]? Which is more effi cient at high [S]?arrow_forwardWhich of the following statements is true about effect of substrate concentration on enzyme activity ? The rate of reaction increases as the substrate concentration increases up to certain limit at which the reaction rate is maximal (Vmax.) At Vmax, the enzyme is completely saturated with the substrate, At Vmax, any increase in substrate concentration don't affect the reaction rate. All of themarrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License