Organic Chemistry (8th Edition)
8th Edition
ISBN: 9780134066639
Author: Bruice
Publisher: PEARSON
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Textbook Question
Chapter 22.9, Problem 16P
Which of the following C-terminal peptide bonds is more readily cleaved by carboxypeptidase A? Explain your choice.
Ser-Ala-Leu or Ser-Ala-Asp
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What fragments are produced when the peptide shown below is treated with trypsin?
Gly-Arg-Val-Phe -Leu-Lys-Met-Trp-Pro-Tyr-Cys-Ser
Explain why, when the guanidino group of arginine is protonated, the double-bonded nitrogen is thenitrogen that accepts the proton.
2 H+ +
NH2NHCH2CH2CH2CHNH
+NH3CO−O
CO−O
H2NC
NHCH2CH2CH2CH
Draw the structure of the N-phenylthiohydantoin formed by initial Edman degradation of each peptide: (a) Ala–Gly–Phe–Phe; (b) Val–Ile–Tyr.
Chapter 22 Solutions
Organic Chemistry (8th Edition)
Ch. 22.2 - Compare each of the mechanisms listed here with...Ch. 22.2 - Prob. 3PCh. 22.2 - Prob. 4PCh. 22.3 - a. Draw the mechanism for the following reaction...Ch. 22.5 - Prob. 7PCh. 22.5 - Propose a mechanism for the Co2+ catalyzed...Ch. 22.6 - Prob. 9PCh. 22.7 - Prob. 10PCh. 22.7 - Prob. 12PCh. 22.7 - Prob. 13P
Ch. 22.9 - Which of the following amino acid side chains can...Ch. 22.9 - Which of the following C-terminal peptide bonds is...Ch. 22.9 - Carboxypeptidase A has esterase activity as well...Ch. 22.10 - Arginine and lysine side chains fit into trypsins...Ch. 22.10 - Explain why serine proteases do not catalyze...Ch. 22.11 - If H2 18O is used in the hydrolysis reaction...Ch. 22.11 - Draw the pH-activity profile for an enzyme that...Ch. 22.12 - The pHactivity profile for glucose-6-phosphate...Ch. 22.12 - Prob. 23PCh. 22.13 - Draw the mechanism for the hydroxide ion-catalyzed...Ch. 22.13 - What advantage does the enzyme gain by forming an...Ch. 22.13 - Prob. 26PCh. 22.13 - Prob. 27PCh. 22.13 - Aldolase shows no activity if it is incubated with...Ch. 22 - Which of the following parameters would be...Ch. 22 - Prob. 29PCh. 22 - Prob. 30PCh. 22 - Prob. 31PCh. 22 - Indicate the type of catalysis that is occurring...Ch. 22 - The deuterium kinetic isotope effect (KH2O/KD2O)...Ch. 22 - Prob. 34PCh. 22 - Co2+ catalyzes the hydrolysis of the lactam shown...Ch. 22 - there are two kinds of aldolases. Class I...Ch. 22 - Prob. 37PCh. 22 - The hydrolysis of the ester shown here is...Ch. 22 - Prob. 39PCh. 22 - At pH = 12, the rate of hydrolysis of ester A is...Ch. 22 - 2-Acetoxycyclohexyl tosylate reacts with acetate...Ch. 22 - Proof that an imine was formed between aldolase...Ch. 22 - Prob. 43PCh. 22 - a. Explain why the alkyl halide shown here reacts...Ch. 22 - Triosephosphate isomerase (TIM) catalyzes the...
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- Explain why serine proteases do not catalyze hydrolysis if the amino acid at the hydrolysis site is a d-amino acid. Trypsin, for example, cleaves on the C-side of L-Arg and L-Lys, but not on the C-side of D-Arg and D-Lys.arrow_forwardShow the mechanism and explain how the Ala-Val-Ile peptide bond is formed.arrow_forwardWhat products are formed when below mentioned peptide is treated with trypsin. Phe–Tyr–Gly–Cys–Arg–Serarrow_forward
- What is the isoelectric point for the peptide MNPQR at pH 7? Draw the structure, including the stereochemistry of each C-alpha chiral center.arrow_forwardWhat type of interaction (IMF) would be present between side chains of the following amino acid residues? Explain your answers. a) 2 phenylalanine residues b) Methionine and valine residues c) Glutamate and arginine residuesarrow_forwardCarboxypeptidase requires a Zn²+ cofactor for the hydrolysis of the peptide bond of a C-terminal aromatic amino acid. T/F?arrow_forward
- What is the structure of a nonapeptide that gives the following fragments when cleaved? Trypsin cleavage: Val-Val-Pro-Tyr-Leu-Arg, Ser-Ile-Arg Chymotrypsin cleavage: Leu-Arg, Ser-Ile-Arg-Val-Val-Pro-Tyrarrow_forwardOxytocin, a nonapeptide hormone secreted by the pituitary gland, functions by stimulating uterine contraction and lactation during childbirth. Its sequence was determined from the following evidence: 1. Oxytocin is a cyclic compound containing a disulfide bridge between two cysteine residues. 2. When the disulfide bridge is reduced, oxytocin has the constitution Asn, Cys2, Gln, Gly, Ile, Leu, Pro, Tyr. 3. Partial hydrolysis of reduced oxytocin yields seven fragments: Asp-Cys, Ile-Glu, Cys-Tyr, Leu-Gly, Tyr-Ile-Glu, Glu-Asp-Cys, and Cys-Pro-Leu. 4. Gly is the C-terminal group. 5. Both Glu and Asp are present as their side-chain amides (Gln and Asn) rather than as free side-chain acids. What is the amino acid sequence of reduced oxytocin? What is the structure of oxytocin itself?arrow_forwardwhich amino acids has a side chain that can serve as a hydrogen bond donor but not acceptor in its predominant form at pH7arrow_forward
- Indicate the peptides produced from cleavage by the indicated reagent: a. His-Lys-Leu-Val-Glu-Pro-Arg-Ala-Gly-Ala by trypsin b. Leu-Gly-Ser-Met-Phe-Pro-Tyr-Gly-Val by chymotrypsinarrow_forwardAfter the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhy-dride, trypsin will cleave the polypeptide only on the C-side of arginine.) Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trparrow_forwardDraw the structure of the following short peptide at pH 7.0. You don't need to show the stereochemistry. Label the peptide bonds, alpha carbons, the C-terminus, and the N-terminus. What is the net charge of this peptide at pH 5.0? Ala-Asn-Glu-Val-Pro-Glyarrow_forward
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