Organic Chemistry
Organic Chemistry
7th Edition
ISBN: 9780321803221
Author: Paula Y. Bruice
Publisher: Prentice Hall
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Chapter 23, Problem 40P
Interpretation Introduction

Interpretation: The mechanism for conversion of carbon dioxide to bicarbonate ion in presence of carbonic anhydrase has to be proposed.

Concept introduction:

  • Enzyme is a protein that is a biological catalyst.  The reactant in a reaction catalyzed by the enzyme is called substrate.  In the enzyme, a pocket like cleft is present called active site where it binds the substrate.
  • Some amino acid chains in the enzyme act as base, acid and nucleophilic catalyst. Many of the enzymes contain metal ions at the active site which acts as catalyst.
  • Acid Catalyst helps in increasing the rate of a particular reaction by the donation of a proton to substrate.
  • Base Catalyst helps in increasing the rate of a particular reaction by the removal of a proton to substrate.
  • Nucleophilic catalysis helps in increasing the rate of a particular reaction by the formation of a covalent bond with substrate
  • Metalloenzyme: An enzyme which has a tightly bound Zn2+ metal ion

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Oxaloacetate is an inhibitor of succinate dehydrogenase because it is structurally very similar to succinate as shown below. Also, its binding to the enzyme does not involve any covalent bond formation. What type of inhibitor is oxaloacetate? COO | CH₂ 1 CH₂ 1 COO Succinate COO | CH₂ C=O COO Oxaloacetate O a noncompetitive inhibitor both a noncompetitive and an irreversible inhibitor O an irreversible inhibitor O a competitive inhibitor
What is the expected result if the enzyme monoamine oxidase is treated with the substrate analog named N,N-dimethylpropargylamine? H3C `N I CH3 N,N-dimethylpropargyl amine The product propargyl aldehyde (H-C=C-CH=O) will be formed and released. The product propargyl alcohol (H-CEC-CH₂-OH will be formed and released. The enzyme will be rapidly and covalently (irreversibly) inhibited. The enzyme will be reversibly and competitively inhibited in the presence of this substrate analog. a. b. monoamine oxidase C. d. MAO + O₂
Consider the following biochemical reactions: HO H₂N A B с NH₂ reaction NH₂ ATP ADP enzyme + 2 H₂O enzyme 0 0 FAD FADH₂ ܘܐ ܀ enzyme type of enzyme needed to catalyze this reaction HO dy dy OH In the table below, write the type of enzyme that catalyzes each reaction. Note: be sure to use only the 6 standard enzyme types. NH₂ + 2 NH3 X Ś A B

Chapter 23 Solutions

Organic Chemistry

Ch. 23.9 - Which of the following amino acid side chains can...Ch. 23.9 - Which of the following C-terminal peptide bonds is...Ch. 23.9 - Carboxypeptidase A has esterase activity as well...Ch. 23.9 - Arginine and lysine side chains fit into trypsins...Ch. 23.9 - Explain why serine proteases do not catalyze...Ch. 23.10 - If H2 18O is used in the hydrolysis reaction...Ch. 23.10 - When apples that have been cut are exposed to...Ch. 23.11 - Prob. 22PCh. 23.11 - The pHactivity profile for glucose-6-phosphate...Ch. 23.11 - Draw the pH-activity profile for an enzyme that...Ch. 23.12 - Prob. 25PCh. 23.12 - Draw the mechanism for the hydroxide ion-catalyzed...Ch. 23.12 - What advantage does the enzyme gain by forming an...Ch. 23.12 - Prob. 28PCh. 23.12 - Aldolase shows no activity if it is incubated with...Ch. 23 - Which of the following parameters would be...Ch. 23 - Prob. 30PCh. 23 - Prob. 31PCh. 23 - Prob. 32PCh. 23 - Indicate the type of catalysis that is occurring...Ch. 23 - The deuterium kinetic isotope effect (KH2O/KD2O)...Ch. 23 - Prob. 35PCh. 23 - Co2+ catalyzes the hydrolysis of the lactam shown...Ch. 23 - there are two kinds of aldolases. Class I...Ch. 23 - Prob. 38PCh. 23 - The hydrolysis of the ester shown here is...Ch. 23 - Prob. 40PCh. 23 - At pH = 12, the rate of hydrolysis of ester A is...Ch. 23 - 2-Acetoxycyclohexyl tosylate reacts with acetate...Ch. 23 - Proof that an imine was formed between aldolase...Ch. 23 - Prob. 44PCh. 23 - a. Explain why the alkyl halide shown here reacts...Ch. 23 - Triosephosphate isomerase (TIM) catalyzes the...
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