(a) Interpretation: Role of Glu 270 in catalysis in the mechanism of carboxypeptidase A should be identified. Concept introduction: Glutamine can also be denoted as Glu 270.It is a general base catalyst in 1 s t step and helps in the catalysis of base whereas it act as general acid catalyst in another step. Glutamine consists of carboxyl group which attacks the hydroxyl of Zn 2 + and thus, it act as a base catalyst that turns into carboxyl group whereas arginine contains ammonium ion which helps in the ionic interaction with the carboxypeptidase. Carboxypeptidase is an enzyme helps in hydrolysis of peptide of proteins and thus converting trypsinogen to trypsin and chymotrypsinogen to chymotrypsin.

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Answer 1

Question

Chapter 8, Problem 9P

Interpretation Introduction

(a) Interpretation:

Role of Glu 270 in catalysis in the mechanism of carboxypeptidase A should be identified.

Concept introduction:

Glutamine can also be denoted as Glu 270.It is a general base catalyst in 1^s^t step and helps in the catalysis of base whereas it act as general acid catalyst in another step.

Glutamine consists of carboxyl group which attacks the hydroxyl of Zn²+ and thus, it act as a base catalyst that turns into carboxyl group whereas arginine contains ammonium ion which helps in the ionic interaction with the carboxypeptidase.

Carboxypeptidase is an enzyme helps in hydrolysis of peptide of proteins and thus converting trypsinogen to trypsin and chymotrypsinogen to chymotrypsin.

Interpretation Introduction

(b) Interpretation:

Role of R 145 in catalysis in the mechanism of carboxypeptidase A should be identified.

Concept introduction:

Arginine having a molar mass of 145contains amino group and ammonium ion. With the help of ammonium ion, the arginine can ionize the substrate by forming a bond with carboxyl group.

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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 8, Problem 9P

Interpretation Introduction

(a) Interpretation:

Role of Glu 270 in catalysis in the mechanism of carboxypeptidase A should be identified.

Concept introduction:

Glutamine can also be denoted as Glu 270.It is a general base catalyst in 1^s^t step and helps in the catalysis of base whereas it act as general acid catalyst in another step.

Glutamine consists of carboxyl group which attacks the hydroxyl of Zn²+ and thus, it act as a base catalyst that turns into carboxyl group whereas arginine contains ammonium ion which helps in the ionic interaction with the carboxypeptidase.

Carboxypeptidase is an enzyme helps in hydrolysis of peptide of proteins and thus converting trypsinogen to trypsin and chymotrypsinogen to chymotrypsin.

Interpretation Introduction

(b) Interpretation:

Role of R 145 in catalysis in the mechanism of carboxypeptidase A should be identified.

Concept introduction:

Arginine having a molar mass of 145contains amino group and ammonium ion. With the help of ammonium ion, the arginine can ionize the substrate by forming a bond with carboxyl group.

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Answer 3

Question

Chapter 8, Problem 9P

Interpretation Introduction

(a) Interpretation:

Role of Glu 270 in catalysis in the mechanism of carboxypeptidase A should be identified.

Concept introduction:

Glutamine can also be denoted as Glu 270.It is a general base catalyst in 1^s^t step and helps in the catalysis of base whereas it act as general acid catalyst in another step.

Glutamine consists of carboxyl group which attacks the hydroxyl of Zn²+ and thus, it act as a base catalyst that turns into carboxyl group whereas arginine contains ammonium ion which helps in the ionic interaction with the carboxypeptidase.

Carboxypeptidase is an enzyme helps in hydrolysis of peptide of proteins and thus converting trypsinogen to trypsin and chymotrypsinogen to chymotrypsin.

Interpretation Introduction

(b) Interpretation:

Role of R 145 in catalysis in the mechanism of carboxypeptidase A should be identified.

Concept introduction:

Arginine having a molar mass of 145contains amino group and ammonium ion. With the help of ammonium ion, the arginine can ionize the substrate by forming a bond with carboxyl group.

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Answer 4

Question

Chapter 8, Problem 9P

Interpretation Introduction

(a) Interpretation:

Role of Glu 270 in catalysis in the mechanism of carboxypeptidase A should be identified.

Concept introduction:

Glutamine can also be denoted as Glu 270.It is a general base catalyst in 1^s^t step and helps in the catalysis of base whereas it act as general acid catalyst in another step.

Glutamine consists of carboxyl group which attacks the hydroxyl of Zn²+ and thus, it act as a base catalyst that turns into carboxyl group whereas arginine contains ammonium ion which helps in the ionic interaction with the carboxypeptidase.

Carboxypeptidase is an enzyme helps in hydrolysis of peptide of proteins and thus converting trypsinogen to trypsin and chymotrypsinogen to chymotrypsin.

Interpretation Introduction

(b) Interpretation:

Role of R 145 in catalysis in the mechanism of carboxypeptidase A should be identified.

Concept introduction:

Arginine having a molar mass of 145contains amino group and ammonium ion. With the help of ammonium ion, the arginine can ionize the substrate by forming a bond with carboxyl group.

Expert Solution & Answer

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Answer 5

Chapter 8, Problem 9P

Interpretation Introduction

(a) Interpretation:

Role of Glu 270 in catalysis in the mechanism of carboxypeptidase A should be identified.

Concept introduction:

Glutamine can also be denoted as Glu 270.It is a general base catalyst in 1^s^t step and helps in the catalysis of base whereas it act as general acid catalyst in another step.

Glutamine consists of carboxyl group which attacks the hydroxyl of Zn²+ and thus, it act as a base catalyst that turns into carboxyl group whereas arginine contains ammonium ion which helps in the ionic interaction with the carboxypeptidase.

Carboxypeptidase is an enzyme helps in hydrolysis of peptide of proteins and thus converting trypsinogen to trypsin and chymotrypsinogen to chymotrypsin.

Interpretation Introduction

(b) Interpretation:

Role of R 145 in catalysis in the mechanism of carboxypeptidase A should be identified.

Concept introduction:

Arginine having a molar mass of 145contains amino group and ammonium ion. With the help of ammonium ion, the arginine can ionize the substrate by forming a bond with carboxyl group.

Answer 6

Chapter 8, Problem 9P

Interpretation Introduction

(a) Interpretation:

Role of Glu 270 in catalysis in the mechanism of carboxypeptidase A should be identified.

Concept introduction:

Glutamine can also be denoted as Glu 270.It is a general base catalyst in 1^s^t step and helps in the catalysis of base whereas it act as general acid catalyst in another step.

Glutamine consists of carboxyl group which attacks the hydroxyl of Zn²+ and thus, it act as a base catalyst that turns into carboxyl group whereas arginine contains ammonium ion which helps in the ionic interaction with the carboxypeptidase.

Carboxypeptidase is an enzyme helps in hydrolysis of peptide of proteins and thus converting trypsinogen to trypsin and chymotrypsinogen to chymotrypsin.

Answer 7

Chapter 8, Problem 9P

Interpretation Introduction

(a) Interpretation:

Role of Glu 270 in catalysis in the mechanism of carboxypeptidase A should be identified.

Concept introduction:

Glutamine can also be denoted as Glu 270.It is a general base catalyst in 1^s^t step and helps in the catalysis of base whereas it act as general acid catalyst in another step.

Glutamine consists of carboxyl group which attacks the hydroxyl of Zn²+ and thus, it act as a base catalyst that turns into carboxyl group whereas arginine contains ammonium ion which helps in the ionic interaction with the carboxypeptidase.

Carboxypeptidase is an enzyme helps in hydrolysis of peptide of proteins and thus converting trypsinogen to trypsin and chymotrypsinogen to chymotrypsin.

Answer 8

Interpretation Introduction

(b) Interpretation:

Role of R 145 in catalysis in the mechanism of carboxypeptidase A should be identified.

Concept introduction:

Arginine having a molar mass of 145contains amino group and ammonium ion. With the help of ammonium ion, the arginine can ionize the substrate by forming a bond with carboxyl group.

Answer 9

Interpretation Introduction

(b) Interpretation:

Role of R 145 in catalysis in the mechanism of carboxypeptidase A should be identified.

Concept introduction:

Arginine having a molar mass of 145contains amino group and ammonium ion. With the help of ammonium ion, the arginine can ionize the substrate by forming a bond with carboxyl group.

Answer 10

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Answer 11

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Answer 12

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Answer 13

Ch. 8 - Prob. 1P Ch. 8 - The enzyme urease catalyzes the hydrolysis of urea...Ch. 8 - An enzyme contains an active site aspartic acid...Ch. 8 - The folding and unfolding rate constants for a...Ch. 8 - In some reactions, in which a protein molecule is...Ch. 8 - Would you expect an “enzyme” designed to bind to...Ch. 8 - The initial rate for an enzyme-catalyzed reaction...Ch. 8 - a. If the total enzyme concentration in Problem 7...Ch. 8 - Prob. 9P Ch. 8 - Prob. 10P

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