Chapter 6, Problem 6H.3E

Interpretation Introduction

Interpretation:

The enzyme-catalyzed conversion of a substrate at ${25}^{o}C$ has a Michaelis constant of $0.015mold{m}^{-3}$ and maximum velocity of $4.25\times {10}^{-4}\text{mol}{\text{dm}}^{\text{-3}}{\text{s}}^{\text{-1}}$ when the enzyme concentration is $3.60\times {10}^{-9}mold{m}^{-3}$. The ${\text{k}}_{\text{cat}}$ and the catalytic efficiency $\eta$ have to be calculated. Wheather the enzyme is catalytically $\left(k_{cat}\right)$ perfect or not has to be found.

Concept Introduction:

The rate of reaction is the quantity of formation of product or the quantity of reactant used per unit time. The rate of reaction doesn’t depend on the sum of amount of reaction mixture used.

The raise in molar concentration of product of a reaction per unit time or decrease in molarity of reactant per unit time is called rate of reaction and is expressed in units of $\text{mol/(L}\text{.s)}$ .

Michaelis-Manten analysis: This is one of the simplest and best known methods of enzyme kinetics.

The model serves to explain how an enzyme can cause kinetic rate enhancement of a reaction and why the rate of a reaction depends on the concentration present.

Michaelis-Manten equation: The equation which describes how reaction velocity varies with substrate concentration.

  $V_o=\frac{V_{\max }\left[S\right]}{K_m+\left[S\right]}$

Where,

$V_o$ is the initial reaction velocity,

$V_{\max }$ is the maximum velocity

$K_m$ is the Michaelis constant =$\left(k_{-1}+k_2\right)/k_1$

$\left[S\right]$ is the substrate concentration.