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:

$\upsilon =\frac{d[P]}{dt}=\frac{V_{\max }[S]}{K_M+[S]}$

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:

$\upsilon =\frac{d[P]}{dt}=\frac{V_{\max }[S]}{K_M+[S]}$

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:

$\upsilon =\frac{d[P]}{dt}=\frac{V_{\max }[S]}{K_M+[S]}$