Organic Chemistry, Books a la Carte Edition (8th Edition)
8th Edition
ISBN: 9780134074580
Author: Bruice, Paula Yurkanis
Publisher: PEARSON
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Chapter 22.10, Problem 19P
Explain why serine proteases do not catalyze hydrolysis if the amino acid at the hydrolysis site is a 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.
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lodoacetamide acts as an irreversible inhibitor for a few enzymes by reacting with the amino acid at the active site having the function group
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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.
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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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- 22-25 Draw the most predominant form of lysine at its isoelectric point.arrow_forwardTrypsin is a digestive enzyme that cleaves proteins into smaller peptide fragments. It does so by hydrolyzing the amide bond (peptide bond) on the C-terminal side of positively-charged amino acids. Draw the three hydrolysis products that result when trypsin reacts with the pentapeptide KINKY at pH 7.4. Recall: the hydrolysis of amide bonds involves the addition of water. Where does the water show up in the products of the reaction?arrow_forwardHumans can synthesize nonessential amino acids from other compounds, whereas essential amino acids must be obtained from the diet. Name the nonessential amino acid that is synthesized in each of the following reactions. COO CH3 COO CH₂ COO™ L CH-NH3* CH₂ CH₂ coo- + 1L de 14 2 COC CH₂ CH₂ coo- COO CH₂ CH₂ doo-arrow_forward
- Lysine and tryptophan are two amino acids that contain an additional N atom in the R group bonded to the α carbon. While lysine is classified as a basic amino acid because it contains an additional basic N atom, tryptophan is classified as a neutral amino acid. Explain why this difference in classification occurs.arrow_forwardThe image below shows an interaction between sulfur atoms on two cysteine amino acid chains. Which milk-derived compound is most likely associated with this interaction? MN-C-2-0- MN-C-2-0- N-C-2-0-N-C-8-0- C₂ SH 2 cysteine O Whey Protein O Casein Proteins O Lactose C₂SH oxidation O Fat Globule Leah4Scl CH₂-S-S-CH₂ cystinearrow_forwardWhich amino acid has the lowest pka? glutamate cysteine asparagine lysinearrow_forward
- If glutamine with labeled nitrogen in the amide group were supplied to the liver undergoing active gluconeogenesis and urea cycle, which of the following sets of molecules is most likely to end up with labeled nitrogen? arginine, citrulline, urea. citrulline, ornithine, glutamate arginine, aspartate, ornithine aspartate, urea, alaninearrow_forward23. Which of the following is NOT a blood group antigenic determinants? L-fucose D-fucose beta-D-N-acetylglucosamine beta-D-N-acetylgalactosamine 24. The six groups of enzymes are the following: I. Oxidoreductases II. Transferases III. Hydrolases IV. Isomerases V. Lyases VI. Ligases Fill in the blanks: _catalyze transfers of groups while catalyze bond breakages.arrow_forward3. What is the product if the following peptide is hydrolyzed? H₂N O OHarrow_forward
- Neostigmine is an inhibitor of acetylcholinesterase. The enzyme attempts to catalyse the same reaction on neostigmine as it does with acetylcholine. However, a stable intermediate is formed which prevents completion of the process and which results in a molecule being covalently linked to the active site. Identify (draw) the stable intermediate and explain why it is stable.arrow_forwardDraw the arrow pushing mechanism of glutamyl - tRNA to glutamate-1 - semialdehydearrow_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_forward
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