(a) To propose: The strong inhibitory property of the peptide pepstatin Introduction: Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

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Answer 1

Question

Chapter 14, Problem 3P

Interpretation Introduction

(a)

To propose:

The strong inhibitory property of the peptide pepstatin

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Interpretation Introduction

(b)

To explain:

Whether the pepstatin exhibit inhibits the HIV-1 protease or not.

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

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The beta-lactamase hydrolyzes the lactam-ring in penicillin. Describe the mechanism of hydrolysis, insuring to include the involvement of S, D, & K in the reaction sequence. Please help

To map the active site of beta-lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Why doesn't D in this hexapeptide not participate in the hydrolysis of the beta-lactam ring even though S, K, and D are involved in the catalyst?

To map the active site of -lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Using the experimental results described above derive the primary sequence of the active site hexapeptide. Please help!

Answer 2

Question

Chapter 14, Problem 3P

Interpretation Introduction

(a)

To propose:

The strong inhibitory property of the peptide pepstatin

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Interpretation Introduction

(b)

To explain:

Whether the pepstatin exhibit inhibits the HIV-1 protease or not.

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

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Answer 3

Question

Chapter 14, Problem 3P

Interpretation Introduction

(a)

To propose:

The strong inhibitory property of the peptide pepstatin

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Interpretation Introduction

(b)

To explain:

Whether the pepstatin exhibit inhibits the HIV-1 protease or not.

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Expert Solution & Answer

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Answer 4

Question

Chapter 14, Problem 3P

Interpretation Introduction

(a)

To propose:

The strong inhibitory property of the peptide pepstatin

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Interpretation Introduction

(b)

To explain:

Whether the pepstatin exhibit inhibits the HIV-1 protease or not.

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

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Answer 5

Chapter 14, Problem 3P

Interpretation Introduction

(a)

To propose:

The strong inhibitory property of the peptide pepstatin

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Interpretation Introduction

(b)

To explain:

Whether the pepstatin exhibit inhibits the HIV-1 protease or not.

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Answer 6

Chapter 14, Problem 3P

Interpretation Introduction

(a)

To propose:

The strong inhibitory property of the peptide pepstatin

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Answer 7

Chapter 14, Problem 3P

Interpretation Introduction

(a)

To propose:

The strong inhibitory property of the peptide pepstatin

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Answer 8

Interpretation Introduction

(b)

To explain:

Whether the pepstatin exhibit inhibits the HIV-1 protease or not.

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Answer 9

Interpretation Introduction

(b)

To explain:

Whether the pepstatin exhibit inhibits the HIV-1 protease or not.

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Answer 10

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Answer 11

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Answer 12

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Answer 13

Ch. 14 - Answers to all problems are at the end Î¿Î“this...Ch. 14 - Answers to all problems are at the end Î¿Î“this...Ch. 14 - Prob. 3P Ch. 14 - Prob. 4P Ch. 14 - Answers to all problems are at the end Î¿Î“this...Ch. 14 - Prob. 6P Ch. 14 - Prob. 7P Ch. 14 - Answers to all problems are at the end Î¿Î“this...Ch. 14 - Answers to all problems are at the end Î¿f this...Ch. 14 - Answers to all problems are at the end Î¿f this...

Solution Summary: The author explains that the strong inhibitory property of pepstatin is due to the transformation of the central amino acid to a transition state.

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