(a) Interpretation: V 0 versus pH curve when the substrate concentration is much greater than the enzyme K M should be drawn. Concept introduction: K M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K M needs a higher concentration of substrate to achieve V max .

Question

Want to see the full answer?

Answer 1

Question

Chapter 8, Problem 46P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Students have asked these similar questions

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 46P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 3

Question

Chapter 8, Problem 46P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 4

Question

Chapter 8, Problem 46P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 5

Chapter 8, Problem 46P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 6

Chapter 8, Problem 46P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 7

Chapter 8, Problem 46P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 8

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 9

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 10

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 11

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

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

Solution Summary: The author explains the Michaelis constant, which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system.

Want to see the full answer?

Chapter 8 Solutions