(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

Enzyme X exhibits maximum activity at pH- 6.3. X shows a fairly sharp decrease in its activity when the pH goes much lower than 5.8. One likely interpretation of this pH activity is that: a Glu residue on the enzyme is involved in the reaction. O the enzyme uses NADH has a cofactor the enzyme uses coenzyme A has a cofactor O a Tyr residue on the enzyme is involved in the reaction. O a His residue on the enzyme is involved in the reaction

8) plot of enzyme activity with and without an inhibitor present gave the following plot. What type of inhibitor is present? How does this inhibitor function? What changes are seen in Vmax and KM? Draw a line that approximates the result from addition of twice as much inhibitor to the reaction. 1/v (v in mM/min) 0.8 0.6 0.4 0.2 0 0.2 0.4 06 1/[s] ([S] in mM) 0.8

molecule A Plot of velocity versus substrate B Lineweaver-Burk plot 1/v Km 1 Vmax (S) Vmx 1 V max 1/2Vmax 1/Vmax -1/Km Km [S] 1/[S] fppt.com molecule Exercise The following data describe an enzyme-catalyzed reaction. Plot these results using the Lineweaver-Burk method, and determine values for KM and Vinax- The symbol mM represents millimoles per liter; 1 mM = 1 × 10 3 mol L. (The concentration of the enzyme is the same in all experiments.) Velocity (mM sec-) Substrate Concentration (тм) 2.5 0.024 5.0 0.036 10.0 0.053 15.0 0.060 20.0 0.061 fppt.com

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