Organic Chemistry, Books a la Carte Edition (8th Edition)
8th Edition
ISBN: 9780134074580
Author: Bruice, Paula Yurkanis
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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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
What products are formed when below mentioned peptide is treated with trypsin.
Phe–Tyr–Gly–Cys–Arg–Ser
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.
Chapter 22 Solutions
Organic Chemistry, Books a la Carte Edition (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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- Show the mechanism and explain how the Ala-Val-Ile peptide bond is formed.arrow_forwardVasopressin is a peptide hormone synthesized by the hypothalamus; in its reduced form it has the structure shown. NH2 HS H H H H H *H3N° NH2 N' SH NH2 ОН Vasopressin NH *H2N= NH2 This structure is incorrect in that one of the amino acids is shown in the D-configuration, rather than the L-. Which one is it? What is the amino acid sequence of this peptide? Enter your answer using the single letter abbretiavions for the amino acids; i.e. GPT, not Gly-Pro-Thr. What is the net charge of this peptide at physiological pH? ZI IZ ZI IZ ZIarrow_forwardWhich of the statements concerning the peptide shown below is FALSE? H2 H3N-C C-N-C- H -O- H2C CH2 CH₂OH H2 Its primary structure is Gly-Pro-Ser. It is a tripeptide. There are two peptide bonds. The peptide contains only hydrophobic amino acid residues.arrow_forward
- After 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_forwardWhich of the following reagents can be used to cleave a tert-butoxycarbonyl (Boc) protecting group from a peptide? H₂/Pd CF3CO₂H Na₂CO3, H₂O LiAlH4 Barrow_forwardDraw the structure of the tetrapeptide Asp-Arg-Val-Tyr. Please show the appropriate stereochemistry of the natural amino acids in the resulting peptide. Please draw all ionizable groups in their neutral form.arrow_forward
- Draw the structure of the pentapeptide Met-Pro-Ser-His-Ile at its plarrow_forwardWhich of the following amous indicates the peptide bond? CA) (B) (C) (D) (E) fut H₂N-CH-C-N-CH-C-OH CHPH H CH3arrow_forwardWhich peptide in below pair has side chains that exhibit predominantly van der Waals forces? Met–Gly–Leu–Phe–Gln–Ala or Lys–Gly–Arg–Tyr–Trp–Gluarrow_forward
- Can someone please help me figure this out and explain how to do them?arrow_forwardReaction of a polypeptide with carboxypeptidase A releases Met. The polypeptide undergoes partial hydrolysis to give the following peptides. What is the sequence of the polypeptide? 1. Ser, Lys, Trp 4. Leu, Glu, Ser 7. Glu, His 10. Glu, His, Val 2. Gly, His, Ala 5. Met, Ala, Gly 8. Leu, Lys, Trp 11. Trp, Leu, Glu 3. Glu, Val, Ser 6. Ser, Lys, Val 9. Lys, Ser 12. Ala, Metarrow_forwardPlease don't provide handwriting solutionarrow_forward
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