(a) Interpretation: The mechanism for peptide bond cleavage by a cysteine protease should be completed. Concept introduction: In peptide bond hydrolysis, the strategy of the protease is to generate a nucleophile that attacks the peptide carbonyl group. In cysteine protease, a cysteine residue is activated by a histidine residue and this activated cysteine act as the nucleophile that attacks the peptide bond.

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Answer 1

Question

Definition Definition Class of organic compounds that contain a carboxyl group ( - COOH ) and has a general formula R - COOH or R - CO 2 H , where R refers to the alkyl, alkenyl, aryl, or other groups. They can undergo different chemical reactions, such as acid-base reactions, esterification, and oxidation. These are essential components of living organisms, playing important roles in metabolic processes, signaling, and as pharmaceuticals.

Chapter 9, Problem 19P

Interpretation Introduction

(a)

Interpretation:

The mechanism for peptide bond cleavage by a cysteine protease should be completed.

Concept introduction:

In peptide bond hydrolysis, the strategy of the protease is to generate a nucleophile that attacks the peptide carbonyl group. In cysteine protease, a cysteine residue is activated by a histidine residue and this activated cysteine act as the nucleophile that attacks the peptide bond.

Interpretation Introduction

(b)

Interpretation:

The mechanism for peptide bond cleavage by an aspartyl protease should be completed.

Concept introduction:

In aspartyl protease active site there are two aspartic residues which allow a water molecule to attack the peptide bond. One aspartic acid residue activates the water molecule, polarizes the peptide carbonyl group so that it is susceptible to attack.

Interpretation Introduction

(c)

Interpretation:

The mechanism for peptide bond cleavage by metalloproteases should be completed.

Concept introduction:

The active site of the metalloprotease is composed of a bound metal ion. This metal ion activates a water molecule in order to perform a nucleophilic attack on peptide carbonyl carbon.

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Answer 2

Question

Definition Definition Class of organic compounds that contain a carboxyl group ( - COOH ) and has a general formula R - COOH or R - CO 2 H , where R refers to the alkyl, alkenyl, aryl, or other groups. They can undergo different chemical reactions, such as acid-base reactions, esterification, and oxidation. These are essential components of living organisms, playing important roles in metabolic processes, signaling, and as pharmaceuticals.

Chapter 9, Problem 19P

Interpretation Introduction

(a)

Interpretation:

The mechanism for peptide bond cleavage by a cysteine protease should be completed.

Concept introduction:

In peptide bond hydrolysis, the strategy of the protease is to generate a nucleophile that attacks the peptide carbonyl group. In cysteine protease, a cysteine residue is activated by a histidine residue and this activated cysteine act as the nucleophile that attacks the peptide bond.

Interpretation Introduction

(b)

Interpretation:

The mechanism for peptide bond cleavage by an aspartyl protease should be completed.

Concept introduction:

In aspartyl protease active site there are two aspartic residues which allow a water molecule to attack the peptide bond. One aspartic acid residue activates the water molecule, polarizes the peptide carbonyl group so that it is susceptible to attack.

Interpretation Introduction

(c)

Interpretation:

The mechanism for peptide bond cleavage by metalloproteases should be completed.

Concept introduction:

The active site of the metalloprotease is composed of a bound metal ion. This metal ion activates a water molecule in order to perform a nucleophilic attack on peptide carbonyl carbon.

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Answer 3

Question

Definition Definition Class of organic compounds that contain a carboxyl group ( - COOH ) and has a general formula R - COOH or R - CO 2 H , where R refers to the alkyl, alkenyl, aryl, or other groups. They can undergo different chemical reactions, such as acid-base reactions, esterification, and oxidation. These are essential components of living organisms, playing important roles in metabolic processes, signaling, and as pharmaceuticals.

Chapter 9, Problem 19P

Interpretation Introduction

(a)

Interpretation:

The mechanism for peptide bond cleavage by a cysteine protease should be completed.

Concept introduction:

In peptide bond hydrolysis, the strategy of the protease is to generate a nucleophile that attacks the peptide carbonyl group. In cysteine protease, a cysteine residue is activated by a histidine residue and this activated cysteine act as the nucleophile that attacks the peptide bond.

Interpretation Introduction

(b)

Interpretation:

The mechanism for peptide bond cleavage by an aspartyl protease should be completed.

Concept introduction:

In aspartyl protease active site there are two aspartic residues which allow a water molecule to attack the peptide bond. One aspartic acid residue activates the water molecule, polarizes the peptide carbonyl group so that it is susceptible to attack.

Interpretation Introduction

(c)

Interpretation:

The mechanism for peptide bond cleavage by metalloproteases should be completed.

Concept introduction:

The active site of the metalloprotease is composed of a bound metal ion. This metal ion activates a water molecule in order to perform a nucleophilic attack on peptide carbonyl carbon.

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Answer 4

Question

Definition Definition Class of organic compounds that contain a carboxyl group ( - COOH ) and has a general formula R - COOH or R - CO 2 H , where R refers to the alkyl, alkenyl, aryl, or other groups. They can undergo different chemical reactions, such as acid-base reactions, esterification, and oxidation. These are essential components of living organisms, playing important roles in metabolic processes, signaling, and as pharmaceuticals.

Chapter 9, Problem 19P

Interpretation Introduction

(a)

Interpretation:

The mechanism for peptide bond cleavage by a cysteine protease should be completed.

Concept introduction:

In peptide bond hydrolysis, the strategy of the protease is to generate a nucleophile that attacks the peptide carbonyl group. In cysteine protease, a cysteine residue is activated by a histidine residue and this activated cysteine act as the nucleophile that attacks the peptide bond.

Interpretation Introduction

(b)

Interpretation:

The mechanism for peptide bond cleavage by an aspartyl protease should be completed.

Concept introduction:

In aspartyl protease active site there are two aspartic residues which allow a water molecule to attack the peptide bond. One aspartic acid residue activates the water molecule, polarizes the peptide carbonyl group so that it is susceptible to attack.

Interpretation Introduction

(c)

Interpretation:

The mechanism for peptide bond cleavage by metalloproteases should be completed.

Concept introduction:

The active site of the metalloprotease is composed of a bound metal ion. This metal ion activates a water molecule in order to perform a nucleophilic attack on peptide carbonyl carbon.

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Answer 5

Chapter 9, Problem 19P

Interpretation Introduction

(a)

Interpretation:

The mechanism for peptide bond cleavage by a cysteine protease should be completed.

Concept introduction:

In peptide bond hydrolysis, the strategy of the protease is to generate a nucleophile that attacks the peptide carbonyl group. In cysteine protease, a cysteine residue is activated by a histidine residue and this activated cysteine act as the nucleophile that attacks the peptide bond.

Interpretation Introduction

(b)

Interpretation:

The mechanism for peptide bond cleavage by an aspartyl protease should be completed.

Concept introduction:

In aspartyl protease active site there are two aspartic residues which allow a water molecule to attack the peptide bond. One aspartic acid residue activates the water molecule, polarizes the peptide carbonyl group so that it is susceptible to attack.

Interpretation Introduction

(c)

Interpretation:

The mechanism for peptide bond cleavage by metalloproteases should be completed.

Concept introduction:

The active site of the metalloprotease is composed of a bound metal ion. This metal ion activates a water molecule in order to perform a nucleophilic attack on peptide carbonyl carbon.

Answer 6

Chapter 9, Problem 19P

Interpretation Introduction

(a)

Interpretation:

The mechanism for peptide bond cleavage by a cysteine protease should be completed.

Concept introduction:

In peptide bond hydrolysis, the strategy of the protease is to generate a nucleophile that attacks the peptide carbonyl group. In cysteine protease, a cysteine residue is activated by a histidine residue and this activated cysteine act as the nucleophile that attacks the peptide bond.

Answer 7

Chapter 9, Problem 19P

Interpretation Introduction

(a)

Interpretation:

The mechanism for peptide bond cleavage by a cysteine protease should be completed.

Concept introduction:

In peptide bond hydrolysis, the strategy of the protease is to generate a nucleophile that attacks the peptide carbonyl group. In cysteine protease, a cysteine residue is activated by a histidine residue and this activated cysteine act as the nucleophile that attacks the peptide bond.

Answer 8

Interpretation Introduction

(b)

Interpretation:

The mechanism for peptide bond cleavage by an aspartyl protease should be completed.

Concept introduction:

In aspartyl protease active site there are two aspartic residues which allow a water molecule to attack the peptide bond. One aspartic acid residue activates the water molecule, polarizes the peptide carbonyl group so that it is susceptible to attack.

Answer 9

Interpretation Introduction

(b)

Interpretation:

The mechanism for peptide bond cleavage by an aspartyl protease should be completed.

Concept introduction:

In aspartyl protease active site there are two aspartic residues which allow a water molecule to attack the peptide bond. One aspartic acid residue activates the water molecule, polarizes the peptide carbonyl group so that it is susceptible to attack.

Answer 10

Interpretation Introduction

(c)

Interpretation:

The mechanism for peptide bond cleavage by metalloproteases should be completed.

Concept introduction:

The active site of the metalloprotease is composed of a bound metal ion. This metal ion activates a water molecule in order to perform a nucleophilic attack on peptide carbonyl carbon.

Answer 11

Interpretation Introduction

(c)

Interpretation:

The mechanism for peptide bond cleavage by metalloproteases should be completed.

Concept introduction:

The active site of the metalloprotease is composed of a bound metal ion. This metal ion activates a water molecule in order to perform a nucleophilic attack on peptide carbonyl carbon.

Answer 12

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Answer 13

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Answer 14

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Answer 15

Ch. 9 - Prob. 1P Ch. 9 - Prob. 2P Ch. 9 - Prob. 3P Ch. 9 - Prob. 4P Ch. 9 - Prob. 5P Ch. 9 - Prob. 6P Ch. 9 - Prob. 7P Ch. 9 - Prob. 8P Ch. 9 - Prob. 9P Ch. 9 - Prob. 10P

Solution Summary: The author explains the mechanism for peptide bond cleavage by a cysteine protease.

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