(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.

Question

Want to see the full answer?

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 17P

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.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Students have asked these similar questions

The preferred substrate is T because the enzyme half-saturates at 7.00 mM for T, but requires 28.0 mM for U, and 112 mM for S. b Question Content Area The rate constant k 2 with substrate S is 9.60×107 sec-1, with substrate T, k 2 = 6.00×104 sec-1, and with substrate U, k 2 = 2.40×106 sec-1. Calculate the catalytic efficiency with S, T, and U. Catalytic efficiency with S = Catalytic efficiency with T = Catalytic efficiency with U = Does enzyme A use substrate S, substrate T, or substrate U with greater catalytic efficiency?

Fumerase catalyzes the conversion of fumerate to malate. fumerate + H2O ⇋ malate The turnover number, kcat, for fumerase is 8.00×102 sec-1. The Km of this enzyme for fumerate is 5.00×10-3 μmol mL-1. a In an experiment using 2.00×10-3 μmol·mL-1, what is Vmax?

Suppose you wanted to make a buffer of exactly pH 7.00 using KH2PO4 and Na2HPO4. If the final solution was 0.18 M in KH2PO4, you would need 0.25 M Na2HPO4. Now assume you wish to make a buffer at the same pH, using the same substances, but want the total phosphate molarity ([HPO42−]+[H2PO−4]) to equal 0.20 M. What concentration of the Na2HPO4 would be required?

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 17P

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.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

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 17P

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.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

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 17P

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.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 5

Chapter 9, Problem 17P

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 17P

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 17P

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

Expert Solution & Answer

Answer 13

Expert Solution & Answer

Answer 14

Want to see the full answer?

Check out a sample textbook solution

See solution

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.

Concept explainers

Videos

Want to see the full answer?

Chapter 9 Solutions