Fundamentals of General, Organic, and Biological Chemistry - With Access
8th Edition
ISBN: 9780134465708
Author: McMurry
Publisher: PEARSON
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Chapter 19, Problem 19.89GP
The ability to change a selected amino acid residue to another amino acid is referred to as “point mutation” by biochemists. Referring to the reaction for peptide bond hydrolysis in Figure 19.4, speculate on the effects that the following point mutations might have on the chymotrypsin mechanism shown in Figure 19.4: serine to valine; aspartate to glutamate.
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What amino acids can be found in chymotrypsin’s specificity pocket? What would happen if one of those amino acids was changed to lysine?
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A mutation that changes an alanine residue in the interior of a protein to valine is found to lead to a loss of activity. However, activity is regained when a second mutation at a different position changes an isoleucine residue to glycine. How might this second mutation lead to a restoration of activity?
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Chapter 19 Solutions
Fundamentals of General, Organic, and Biological Chemistry - With Access
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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- Name the α-ketoacid that is formed by the transamination of each of the following amino acids: (a) Alanine (d) Leucine (b) Aspartate (e) Phenylalanine (c) Glutamate (f) Tyrosinearrow_forwardIn a paragraph form, provide the experimental procedures in removal of the carbon dioxide present in the mechanism of reaction of protein that contain native serine residues by the reaction of oxazetidine-containing peptides and α-ketoacidarrow_forwardWhich of the following is an example of an unacceptable missense? a. HbA is converted to Hb Hikari, where the beta chain Lysine at #61 is replaced by Asparagine. b. Hb A, is converted to Hb M (Boston) where the alpha chain Histidine at #58 is replaced by Tyrosine. c. Hb A is converted to Hb S, where the beta chain Glutamate at #6 is replaced by Valine.arrow_forward
- Illustrate the pathways to synthesize the following amino acids: glutamine, serine, arginine, glycine, and cysteine.arrow_forwardName and draw the structure of the a-keto acid resulting when each of the following amino acids undergoes transamination with a-ketoglutarate: (a) aspartate, (b) glutamate, (c) alanine, (d) phenylalanine.arrow_forwardIllustrate the pathways to synthesize the following aminoacids:a. glutamineb. serinec. arginined. glycinee. cysteinearrow_forward
- Under certain conditions, peptide bond formation is more thermodynamically favorable than peptide bond hydrolysis. Would you expect chymotrypsin to catalyze peptide bond formation?arrow_forwardExplain all amin acids are absorbed in L- form while methionine as amino acid absorbed in D-form?arrow_forwardWhich of the following statements is not true about the catalytic triad in chymotrypsin? Group of answer choices the side chain of the serine 195 is hydrogen bonded to the imidazole ring of histidine the -NH group of the imidazole ring of histidine is hydrogen bonded to the carboxylate group of aspartate 102 the histidine residue serves to position the aspartate 102 side chain and to polarize its carboxylate group so that it is poised for deprotonation histidine acts as a general base catalyst none of thesearrow_forward
- A tripeptide has the following sequence: Glu-Trp-Arg What is the net charge of this tripeptide at physiological pH?arrow_forwardUsing the catalytic mechanism of serine proteases, draw and label a reaction coordinate diagram/graph of the chymotrypsin-catalyzed hydrolysis of a peptide bond.arrow_forwardThroughout the polypeptide chain, must the amino acid residues at the active site be next to one another? Explain.arrow_forward
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