Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
8th Edition
ISBN: 9780134015187
Author: John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher: PEARSON
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Textbook Question
Chapter 19, Problem 19.29AP
Explain how the following mechanisms regulate enzyme activity.
- (a) Covalent modification
- (b) Genetic control
- (c) Allosteric regulation
- (d) Feedback inhibition
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1. Allosteric regulation is an important part of feedback regulation. All of the functions listed below can be performed by an allosteric molecule EXCEPT: A) catalysis of a reaction. B) activation of an enzyme. C) inhibition of an enzyme. D) conformational change of an enzyme.
(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.
(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.
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Chapter 19 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
Ch. 19.1 - Prob. 19.1PCh. 19.1 - The enzyme LDH converts lactate to pyruvate. In...Ch. 19.2 - The cofactors NAD+, Cu2+, Zn2+, coenzyme A, FAD,...Ch. 19.3 - Describe the reactions that you would expect these...Ch. 19.3 - Prob. 19.5PCh. 19.3 - Prob. 19.6PCh. 19.3 - Prob. 19.7PCh. 19.3 - Prob. 19.8PCh. 19.4 - Prob. 19.9KCPCh. 19.5 - Prob. 19.10KCP
Ch. 19.5 - Prob. 19.11PCh. 19.5 - Prob. 19.12PCh. 19.6 - Prob. 19.13PCh. 19.6 - Prob. 19.14PCh. 19.7 - (a) L-Threonine is converted to L-isoleucine in a...Ch. 19.8 - AZT (zidovudine) inhibits the synthesis of the HIV...Ch. 19.8 - Prob. 19.3CIAPCh. 19.8 - Prob. 19.16PCh. 19.9 - Does the enzyme described in each of the following...Ch. 19.9 - Prob. 19.18PCh. 19.9 - Compare the structures of vitamin A and vitamin C....Ch. 19.9 - Prob. 19.20PCh. 19.9 - Prob. 19.21KCPCh. 19.9 - Prob. 19.22PCh. 19.9 - Prob. 19.4CIAPCh. 19.9 - Prob. 19.6CIAPCh. 19.9 - Prob. 19.7CIAPCh. 19.9 - Enzyme levels in blood are often elevated in...Ch. 19.9 - Prob. 19.9CIAPCh. 19.9 - Prob. 19.23PCh. 19 - Prob. 19.24UKCCh. 19 - Prob. 19.25UKCCh. 19 - Prob. 19.26UKCCh. 19 - Prob. 19.27UKCCh. 19 - Prob. 19.28APCh. 19 - Explain how the following mechanisms regulate...Ch. 19 - Prob. 19.30APCh. 19 - Prob. 19.31APCh. 19 - Prob. 19.32APCh. 19 - Prob. 19.33APCh. 19 - Prob. 19.34APCh. 19 - Prob. 19.35APCh. 19 - Prob. 19.36APCh. 19 - Prob. 19.37APCh. 19 - Name an enzyme that acts on each molecule. (a)...Ch. 19 - Name an enzyme that acts on each molecule. (a)...Ch. 19 - What features of enzymes make them so specific in...Ch. 19 - Describe in general terms how enzymes act as...Ch. 19 - Prob. 19.42APCh. 19 - Prob. 19.43APCh. 19 - Prob. 19.44APCh. 19 - Prob. 19.45APCh. 19 - Prob. 19.46APCh. 19 - Prob. 19.47APCh. 19 - What is the difference between the lock-and-key...Ch. 19 - Why is the induced-fit model a more likely model...Ch. 19 - Prob. 19.50APCh. 19 - Prob. 19.51APCh. 19 - How do you explain the observation that pepsin, a...Ch. 19 - Prob. 19.53APCh. 19 - Prob. 19.54APCh. 19 - Prob. 19.55APCh. 19 - Prob. 19.56APCh. 19 - Prob. 19.57APCh. 19 - The text discusses three forms of enzyme...Ch. 19 - Prob. 19.59APCh. 19 - Prob. 19.60APCh. 19 - Prob. 19.62APCh. 19 - Prob. 19.63APCh. 19 - The meat tenderizer used in cooking is primarily...Ch. 19 - Prob. 19.65APCh. 19 - Why do allosteric enzymes have two types of...Ch. 19 - Prob. 19.67APCh. 19 - Prob. 19.68APCh. 19 - Prob. 19.69APCh. 19 - Prob. 19.70APCh. 19 - Prob. 19.71APCh. 19 - Prob. 19.72APCh. 19 - Prob. 19.73APCh. 19 - Prob. 19.74APCh. 19 - Prob. 19.75APCh. 19 - Prob. 19.76APCh. 19 - Prob. 19.77APCh. 19 - Prob. 19.78APCh. 19 - Prob. 19.79APCh. 19 - Prob. 19.80CPCh. 19 - Prob. 19.81CPCh. 19 - Prob. 19.82CPCh. 19 - Prob. 19.83CPCh. 19 - Prob. 19.84CPCh. 19 - Prob. 19.85CPCh. 19 - Prob. 19.86CPCh. 19 - Prob. 19.87CPCh. 19 - Prob. 19.88GPCh. 19 - The ability to change a selected amino acid...Ch. 19 - Prob. 19.90GPCh. 19 - Prob. 19.91GP
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- A competitive inhibitor diminishes the rate of catalysis: A) By reducing the proportion of enzyme molecules bound to a substrate. OB) By altering the shape of the active site of the enzyme C) By binding to a regulatory subunit D) By enhancing the interaction between enzyme and reaction productarrow_forwardBen is studying an enzyme-catalyzed reaction. In the reaction, H+ ions are formed. He found that after a specific time, the reaction stopped, even though there was still a lot of substrate available in the mixture. a) Propose a hypothesis to explain why the reaction stopped.arrow_forward“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 darrow_forward
- Which of the following statements is/are correct?a) Enzyme quantities depend on the rate of their synthesis and degradationb) Enzyme quantity is decreased if an amino-acid involved in the catalytic activity is modifiedc) Protein kinase A activity is regulated through protein interaction.d) Kinases control the activity of other enzymes by covalent modification; irreversiblephosphorylation explain each of the following optionarrow_forwardWhich of the following statement regarding enzymes is false? a.) they speed up reaction rates b.) they work within narrow temperature and pH ranges c.) The active site binds the substarate d.) They are consumed in the reactions they catalyzearrow_forwarda) Describe a specific chemical reaction that occurs within the human body and state the name of the enzyme involved, the substrate(s) of the reaction, and the specific product(s) formed. b) Enzymes are not used up in chemical reactions. So, what exactly does an enzyme do? In your answer you should refer to activation energy. c) Explain what is meant by the induced fit action of an enzyme, referring to the role of the active site, and to the activation energy of an enzyme-catalysed reaction.arrow_forward
- Choose the best description of an enzyme: (a) It allows a chemical reaction to proceed extremely fast. (b) It increases the rate at which a chemical reaction approaches equilibrium relative to its uncatalyzed rate. (c) It makes a reaction thermodynamically favorable.arrow_forwardIn the metabolic pathway, A->B->C->D->E what effect would molecule E likely have on the enzyme that catalyzes A->B? (The answer is A. Could you justify the reason why the answer is A?) a) Allosteric inhibitor b)Allosteric activator c) Competitive inhibitor d) feedback activator e) coenzymearrow_forwardQ: Select the features of the structure and functioning of allosteric enzymes: a) are metabolic pathway limiting enzymes b) when interacting with ligands do not show a cooperative effect c) are monomeric proteins d) have spatially separated active and regulatory centers e) do not exhibit regulatory properties during dissociation of the molecule into protomersarrow_forward
- Which statement best summarizes the structure of an enzyme before and after it catalyzes a reaction? a.) Its structure is the same. b.) It gains a water molecule in the reaction. c.) It loses a carbon atom in the reaction. d.) It loses a hydrogen atom in the reaction,arrow_forwardThe text discusses three forms of enzyme inhibition: uncompetitive inhibition, competitive inhibition, and irreversible inhibition.(a) Describe how an enzyme inhibitor of each type works.(b) What kinds of bonds are formed between an enzymeand each of these three kinds of inhibitors?arrow_forwardQ: The activation of allosteric enzymes leads to: a) dissociation of protomers upon breaking weak bonds b) hydrolysis of peptide bonds c) phosphorylation of enzyme molecules d) cooperative interaction of subunits e) chemical modification of the enzymearrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License