Organic Chemistry (8th Edition)
Organic Chemistry (8th Edition)
8th Edition
ISBN: 9780134042282
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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Chapter 22.12, Problem 23P
Interpretation Introduction

Interpretation: The reason for why mannose is not formed in the enzyme catalyzed reaction and mannose is one of the products when glucose undergoes base-catalyzed isomerization in the absence of a catalyst has to be explained

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
  • Glycolysis: A series of reactions where glucose is converted to two pyruvate molecules in the presence of enzymes catalysis.

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Q5:
Find an example of an enzyme. a) What is the chemical reaction that is catalyzed by the enzyme? b) Why is this enzyme/chemical reaction important to the organisms in which it occurs?
Enzymes function most efficiently at the temperature of a typical cell, which is 37 degrees Celsius. Increases or decreases in temperature can significantly lower the reaction rate. What does this suggest about the importance of temperature-regulating mechanisms in organisms? How does this translate to the development of enzyme assays for clinical laboratory testing equipment? Explain.

Chapter 22 Solutions

Organic Chemistry (8th Edition)

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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