The reason behind not being the concentration of finding K m and V max on the constant spaced x-axis of the graph. Introduction: Enzymes are “biocatalysts” which takes part in a process and alters the rate of reaction . The enzymes work on the entity known as “substrates” and after having interaction with the substrate is converted into the “product.” The K m of an enzyme can be described as the amount of substrate required for the purpose of saturation. Whereas, when the rate of reaction is at the top, the condition is known as V max .

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Answer 1

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Chapter 6, Problem 1Q

Summary Introduction

To determine: The reason behind not being the concentration of finding K_m and V_max on the constant spaced x-axis of the graph.

Introduction: Enzymes are “biocatalysts” which takes part in a process and alters the rate of reaction. The enzymes work on the entity known as “substrates” and after having interaction with the substrate is converted into the “product.” The K_m of an enzyme can be described as the amount of substrate required for the purpose of saturation. Whereas, when the rate of reaction is at the top, the condition is known as V_max.

Summary Introduction

To suggest: An improvement in the graph.

Introduction: Enzymes are “biocatalysts” which takes part in a process and alters the rate of reaction. The enzymes work on the entity known as “substrates” and after having interaction with the substrate is converted into the “product.” The K_m of an enzyme can be described as the amount of substrate required for the purpose of saturation. Whereas, when the rate of reaction is at the top, the condition is known as V_max.

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Staphylococcal nuclease has a ΔΔG‡ of -84.1 kJ mol-1 at 25.0 °C. If the uncatalyzed rate is 0.630x10-13 µmol s-1, calculate the enzyme-catalyzed rate in µmol s-1. (Use R = 8.3145 J mol-1 K-1)

An enzyme-catalyzed reaction has a KM of 20.0 mmol L-1 and Vmax of 17.0 pmol s-1. When a mixed inhibitor is added, the apparent KM is 50.0 mmol L-1 and the apparent Vmax is 5.20 pmol s-1. Calculate α.

The enzyme β-methylaspartase catalyzes the deamination of β-methylaspartate. For this aspartate reaction in the presence of the inhibitor hydroxymethylaspartate (3.8 M), determine KM and whether the inhibition is competitive or noncompetitive (KI = 1.0 M). In the ABSENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= __________ (1[S])(1[S]) + __________, and the KM is __________ M. In the PRESENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= ____________ (1[S])(1[S]) + ___________, and the KM is ___________ M. The type of inhibition is ____________. Round-off all answers to two (2) significant figures.

Answer 2

Question

Chapter 6, Problem 1Q

Summary Introduction

To determine: The reason behind not being the concentration of finding K_m and V_max on the constant spaced x-axis of the graph.

Introduction: Enzymes are “biocatalysts” which takes part in a process and alters the rate of reaction. The enzymes work on the entity known as “substrates” and after having interaction with the substrate is converted into the “product.” The K_m of an enzyme can be described as the amount of substrate required for the purpose of saturation. Whereas, when the rate of reaction is at the top, the condition is known as V_max.

Summary Introduction

To suggest: An improvement in the graph.

Introduction: Enzymes are “biocatalysts” which takes part in a process and alters the rate of reaction. The enzymes work on the entity known as “substrates” and after having interaction with the substrate is converted into the “product.” The K_m of an enzyme can be described as the amount of substrate required for the purpose of saturation. Whereas, when the rate of reaction is at the top, the condition is known as V_max.

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Answer 3

Question

Chapter 6, Problem 1Q

Summary Introduction

To determine: The reason behind not being the concentration of finding K_m and V_max on the constant spaced x-axis of the graph.

Introduction: Enzymes are “biocatalysts” which takes part in a process and alters the rate of reaction. The enzymes work on the entity known as “substrates” and after having interaction with the substrate is converted into the “product.” The K_m of an enzyme can be described as the amount of substrate required for the purpose of saturation. Whereas, when the rate of reaction is at the top, the condition is known as V_max.

Summary Introduction

To suggest: An improvement in the graph.

Introduction: Enzymes are “biocatalysts” which takes part in a process and alters the rate of reaction. The enzymes work on the entity known as “substrates” and after having interaction with the substrate is converted into the “product.” The K_m of an enzyme can be described as the amount of substrate required for the purpose of saturation. Whereas, when the rate of reaction is at the top, the condition is known as V_max.

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Answer 4

Question

Chapter 6, Problem 1Q

Summary Introduction

To determine: The reason behind not being the concentration of finding K_m and V_max on the constant spaced x-axis of the graph.

Introduction: Enzymes are “biocatalysts” which takes part in a process and alters the rate of reaction. The enzymes work on the entity known as “substrates” and after having interaction with the substrate is converted into the “product.” The K_m of an enzyme can be described as the amount of substrate required for the purpose of saturation. Whereas, when the rate of reaction is at the top, the condition is known as V_max.

Summary Introduction

To suggest: An improvement in the graph.

Introduction: Enzymes are “biocatalysts” which takes part in a process and alters the rate of reaction. The enzymes work on the entity known as “substrates” and after having interaction with the substrate is converted into the “product.” The K_m of an enzyme can be described as the amount of substrate required for the purpose of saturation. Whereas, when the rate of reaction is at the top, the condition is known as V_max.

Expert Solution & Answer

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Answer 5

Chapter 6, Problem 1Q

Summary Introduction

To determine: The reason behind not being the concentration of finding K_m and V_max on the constant spaced x-axis of the graph.

Introduction: Enzymes are “biocatalysts” which takes part in a process and alters the rate of reaction. The enzymes work on the entity known as “substrates” and after having interaction with the substrate is converted into the “product.” The K_m of an enzyme can be described as the amount of substrate required for the purpose of saturation. Whereas, when the rate of reaction is at the top, the condition is known as V_max.

Summary Introduction

To suggest: An improvement in the graph.

Introduction: Enzymes are “biocatalysts” which takes part in a process and alters the rate of reaction. The enzymes work on the entity known as “substrates” and after having interaction with the substrate is converted into the “product.” The K_m of an enzyme can be described as the amount of substrate required for the purpose of saturation. Whereas, when the rate of reaction is at the top, the condition is known as V_max.

Answer 6

Chapter 6, Problem 1Q

Summary Introduction

To determine: The reason behind not being the concentration of finding K_m and V_max on the constant spaced x-axis of the graph.

Introduction: Enzymes are “biocatalysts” which takes part in a process and alters the rate of reaction. The enzymes work on the entity known as “substrates” and after having interaction with the substrate is converted into the “product.” The K_m of an enzyme can be described as the amount of substrate required for the purpose of saturation. Whereas, when the rate of reaction is at the top, the condition is known as V_max.

Answer 7

Chapter 6, Problem 1Q

Summary Introduction

To determine: The reason behind not being the concentration of finding K_m and V_max on the constant spaced x-axis of the graph.

Introduction: Enzymes are “biocatalysts” which takes part in a process and alters the rate of reaction. The enzymes work on the entity known as “substrates” and after having interaction with the substrate is converted into the “product.” The K_m of an enzyme can be described as the amount of substrate required for the purpose of saturation. Whereas, when the rate of reaction is at the top, the condition is known as V_max.

Answer 8

Summary Introduction

To suggest: An improvement in the graph.

Introduction: Enzymes are “biocatalysts” which takes part in a process and alters the rate of reaction. The enzymes work on the entity known as “substrates” and after having interaction with the substrate is converted into the “product.” The K_m of an enzyme can be described as the amount of substrate required for the purpose of saturation. Whereas, when the rate of reaction is at the top, the condition is known as V_max.

Answer 9

Summary Introduction

To suggest: An improvement in the graph.

Introduction: Enzymes are “biocatalysts” which takes part in a process and alters the rate of reaction. The enzymes work on the entity known as “substrates” and after having interaction with the substrate is converted into the “product.” The K_m of an enzyme can be described as the amount of substrate required for the purpose of saturation. Whereas, when the rate of reaction is at the top, the condition is known as V_max.

Answer 10

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Answer 13

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Solution Summary: The author explains that the concentration of finding K m and V max on the constant spaced x-axis of the graph is not the best set of concentration because the uniformly distributed points in reference to figure 6B-1 are

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