(a) Interpretation: K cat and K M values should be determined. Concept introduction: The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below: υ = d [ P ] d t = V max [ S ] K M + [ S ]

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Answer 1

Question

Chapter 36, Problem 17P

Interpretation Introduction

(a)

Interpretation:

K_cat and K_M values should be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Interpretation Introduction

(b)

Interpretation:

Step size for myosin V should be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Interpretation Introduction

(c)

Interpretation:

The processive motion of the myosin V enzyme must be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

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The preferred substrate is T because the enzyme half-saturates at 7.00 mM for T, but requires 28.0 mM for U, and 112 mM for S. b Question Content Area The rate constant k 2 with substrate S is 9.60×107 sec-1, with substrate T, k 2 = 6.00×104 sec-1, and with substrate U, k 2 = 2.40×106 sec-1. Calculate the catalytic efficiency with S, T, and U. Catalytic efficiency with S = Catalytic efficiency with T = Catalytic efficiency with U = Does enzyme A use substrate S, substrate T, or substrate U with greater catalytic efficiency?

Fumerase catalyzes the conversion of fumerate to malate. fumerate + H2O ⇋ malate The turnover number, kcat, for fumerase is 8.00×102 sec-1. The Km of this enzyme for fumerate is 5.00×10-3 μmol mL-1. a In an experiment using 2.00×10-3 μmol·mL-1, what is Vmax?

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Answer 2

Question

Chapter 36, Problem 17P

Interpretation Introduction

(a)

Interpretation:

K_cat and K_M values should be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Interpretation Introduction

(b)

Interpretation:

Step size for myosin V should be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Interpretation Introduction

(c)

Interpretation:

The processive motion of the myosin V enzyme must be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

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Check out a sample textbook solution

See solution

Answer 3

Question

Chapter 36, Problem 17P

Interpretation Introduction

(a)

Interpretation:

K_cat and K_M values should be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Interpretation Introduction

(b)

Interpretation:

Step size for myosin V should be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Interpretation Introduction

(c)

Interpretation:

The processive motion of the myosin V enzyme must be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Expert Solution & Answer

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Check out a sample textbook solution

See solution

Answer 4

Question

Chapter 36, Problem 17P

Interpretation Introduction

(a)

Interpretation:

K_cat and K_M values should be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Interpretation Introduction

(b)

Interpretation:

Step size for myosin V should be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Interpretation Introduction

(c)

Interpretation:

The processive motion of the myosin V enzyme must be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Expert Solution & Answer

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Check out a sample textbook solution

See solution

Answer 5

Chapter 36, Problem 17P

Interpretation Introduction

(a)

Interpretation:

K_cat and K_M values should be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Interpretation Introduction

(b)

Interpretation:

Step size for myosin V should be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Interpretation Introduction

(c)

Interpretation:

The processive motion of the myosin V enzyme must be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Answer 6

Chapter 36, Problem 17P

Interpretation Introduction

(a)

Interpretation:

K_cat and K_M values should be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Answer 7

Chapter 36, Problem 17P

Interpretation Introduction

(a)

Interpretation:

K_cat and K_M values should be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Answer 8

Interpretation Introduction

(b)

Interpretation:

Step size for myosin V should be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Answer 9

Interpretation Introduction

(b)

Interpretation:

Step size for myosin V should be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Answer 10

Interpretation Introduction

(c)

Interpretation:

The processive motion of the myosin V enzyme must be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Answer 11

Interpretation Introduction

(c)

Interpretation:

The processive motion of the myosin V enzyme must be determined.

Concept introduction:

The Michaelis-Menten kinetics is the best model for the enzyme kinetics. This model describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration, [S]. The Michaelis-Menten equation is shown below:

υ=d[P]dt=Vmax[S]KM+[S]

Answer 12

Expert Solution & Answer

Answer 13

Expert Solution & Answer

Answer 14

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Answer 15

Ch. 36 - Prob. 1P Ch. 36 - Prob. 2P Ch. 36 - Prob. 3P Ch. 36 - Prob. 4P Ch. 36 - Prob. 5P Ch. 36 - Prob. 6P Ch. 36 - Prob. 7P Ch. 36 - Prob. 8P Ch. 36 - Prob. 9P Ch. 36 - Prob. 10P

Solution Summary: The author explains the Michaelis-Menten kinetics, which describes the enzymatic reactions by relating rate of the reaction (v) to the substrate concentration.

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Chapter 36 Solutions