The type of inhibition when 5nM of reversible inhibitor yields a V max of 80% of value in the absence of the inhibitor and the KM value is unchanged. Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K M is the Michaelis-Menton constant. K M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V max is the maximum velocity which the enzyme catalyzes the reaction.

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Answer 1

Question

Chapter 12, Problem 29CQ

(a)

Summary Introduction

To explain: The type of inhibition when 5nM of reversible inhibitor yields a V_max of 80% of value in the absence of the inhibitor and the KM value is unchanged.

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

(b)

Summary Introduction

To explain: The proportion of enzyme molecules bound to the inhibitor when 5nM of reversible inhibitor yields a V_max of 80% of value in the absence of the inhibitor.

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

(c)

Summary Introduction

To calculate: Inhibition constant

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

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Answer 2

Question

Chapter 12, Problem 29CQ

(a)

Summary Introduction

To explain: The type of inhibition when 5nM of reversible inhibitor yields a V_max of 80% of value in the absence of the inhibitor and the KM value is unchanged.

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

(b)

Summary Introduction

To explain: The proportion of enzyme molecules bound to the inhibitor when 5nM of reversible inhibitor yields a V_max of 80% of value in the absence of the inhibitor.

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

(c)

Summary Introduction

To calculate: Inhibition constant

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

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Answer 3

Question

Chapter 12, Problem 29CQ

(a)

Summary Introduction

To explain: The type of inhibition when 5nM of reversible inhibitor yields a V_max of 80% of value in the absence of the inhibitor and the KM value is unchanged.

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

(b)

Summary Introduction

To explain: The proportion of enzyme molecules bound to the inhibitor when 5nM of reversible inhibitor yields a V_max of 80% of value in the absence of the inhibitor.

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

(c)

Summary Introduction

To calculate: Inhibition constant

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

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Answer 4

Question

Chapter 12, Problem 29CQ

(a)

Summary Introduction

To explain: The type of inhibition when 5nM of reversible inhibitor yields a V_max of 80% of value in the absence of the inhibitor and the KM value is unchanged.

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

(b)

Summary Introduction

To explain: The proportion of enzyme molecules bound to the inhibitor when 5nM of reversible inhibitor yields a V_max of 80% of value in the absence of the inhibitor.

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

(c)

Summary Introduction

To calculate: Inhibition constant

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

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Answer 5

Chapter 12, Problem 29CQ

(a)

Summary Introduction

To explain: The type of inhibition when 5nM of reversible inhibitor yields a V_max of 80% of value in the absence of the inhibitor and the KM value is unchanged.

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

(b)

Summary Introduction

To explain: The proportion of enzyme molecules bound to the inhibitor when 5nM of reversible inhibitor yields a V_max of 80% of value in the absence of the inhibitor.

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

(c)

Summary Introduction

To calculate: Inhibition constant

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

Answer 6

Chapter 12, Problem 29CQ

(a)

Summary Introduction

To explain: The type of inhibition when 5nM of reversible inhibitor yields a V_max of 80% of value in the absence of the inhibitor and the KM value is unchanged.

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

Answer 7

Chapter 12, Problem 29CQ

(a)

Summary Introduction

To explain: The type of inhibition when 5nM of reversible inhibitor yields a V_max of 80% of value in the absence of the inhibitor and the KM value is unchanged.

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

Answer 8

(b)

Summary Introduction

To explain: The proportion of enzyme molecules bound to the inhibitor when 5nM of reversible inhibitor yields a V_max of 80% of value in the absence of the inhibitor.

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

Answer 9

(b)

Summary Introduction

To explain: The proportion of enzyme molecules bound to the inhibitor when 5nM of reversible inhibitor yields a V_max of 80% of value in the absence of the inhibitor.

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

Answer 10

(c)

Summary Introduction

To calculate: Inhibition constant

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

Answer 11

(c)

Summary Introduction

To calculate: Inhibition constant

Concept introduction: Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. Enzyme inhibitors are those that block the enzyme activity. K_M is the Michaelis-Menton constant. K_M value is not a direct measure of the affinity of the enzyme towards the substrate, but the concentration of S, where the velocity at maximum is half. V_max is the maximum velocity which the enzyme catalyzes the reaction.

Answer 12

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Answer 15

Ch. 12 - Prob. 1E Ch. 12 - Prob. 2E Ch. 12 - Prob. 3E Ch. 12 - Prob. 4E Ch. 12 - 5. From the reaction data below, determine whether...Ch. 12 - Prob. 6E Ch. 12 - 7. For an enzymatic reaction, draw curves that...Ch. 12 - 8. Explain why it is usually easier to calculate...Ch. 12 - Prob. 9E Ch. 12 - 10. Identify the enzymes in Table 12-1 whose...

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