Reason for why glucose-6-phosphate gets isomerized to fructose-6-phosphate before the cleavage reaction with aldolase during glycolysis 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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Answer 1

Question

Chapter 18, Problem 41P

Interpretation Introduction

Interpretation:

Reason for why glucose-6-phosphate gets isomerized to fructose-6-phosphate before the cleavage reaction with aldolase during glycolysis 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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Answer 2

Question

Chapter 18, Problem 41P

Interpretation Introduction

Interpretation:

Reason for why glucose-6-phosphate gets isomerized to fructose-6-phosphate before the cleavage reaction with aldolase during glycolysis 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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Answer 3

Question

Chapter 18, Problem 41P

Interpretation Introduction

Interpretation:

Reason for why glucose-6-phosphate gets isomerized to fructose-6-phosphate before the cleavage reaction with aldolase during glycolysis 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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Answer 4

Question

Chapter 18, Problem 41P

Interpretation Introduction

Interpretation:

Reason for why glucose-6-phosphate gets isomerized to fructose-6-phosphate before the cleavage reaction with aldolase during glycolysis 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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Answer 5

Chapter 18, Problem 41P

Interpretation Introduction

Interpretation:

Reason for why glucose-6-phosphate gets isomerized to fructose-6-phosphate before the cleavage reaction with aldolase during glycolysis 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.

Answer 6

Chapter 18, Problem 41P

Interpretation Introduction

Interpretation:

Reason for why glucose-6-phosphate gets isomerized to fructose-6-phosphate before the cleavage reaction with aldolase during glycolysis 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.

Answer 7

Chapter 18, Problem 41P

Interpretation Introduction

Interpretation:

Reason for why glucose-6-phosphate gets isomerized to fructose-6-phosphate before the cleavage reaction with aldolase during glycolysis 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.

Answer 8

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Answer 9

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Answer 10

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Answer 11

Ch. 18.1 - Prob. 1P Ch. 18.2 - If H218O were used to hydrolyze lysozyme, which...Ch. 18.3 - Which of the following amino acid side chains can...Ch. 18.3 - Arginine and lysine side chains fit into trypsins...Ch. 18.4 - Which of the following amino acid side chains can...Ch. 18.4 - Prob. 6P Ch. 18.5 - Prob. 7P Ch. 18.5 - Draw the mechanism for the hydroxide-ion-catalyzed...Ch. 18.5 - What advantage does the enzyme gain by forming an...Ch. 18.7 - Prob. 10P

Solution Summary: The author explains the mechanism by which glucose-6-phosphate gets isomerized to fructose, before cleavage reaction with aldolase during glycolysis.

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Chapter 18 Solutions