EBK ORGANIC CHEMISTRY
EBK ORGANIC CHEMISTRY
8th Edition
ISBN: 8220102744127
Author: Bruice
Publisher: PEARSON
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Chapter 22, Problem 39P
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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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
ki k3 Q2/ For the following Enzyme catalysis reaction: E+SES E+P K2 find the rate law at low and high concentration of substrate
Consider the reaction. k₁ S P k₂ What effects are produced by an enzyme on the general reaction? AG for the reaction increases. The formation of the transition state is promoted. The reaction equilibrium is shifted toward the products. The concentration of the reactants is decreased. The activation energy for the reaction is lowered. The rate constant for the forward reaction (k₁1) increases.

Chapter 22 Solutions

EBK ORGANIC CHEMISTRY

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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