Chapter 12, Problem 12E

Summary Introduction

To explain: The reason why the given sets of Lineweaver-Burk plots are not individually ideal for determining K_M for an enzyme-catalyzed reaction that follows Michaeli-Menten kinetics.

Concept introduction:

Enzymes are biological protein catalysts which alter the speed of the reaction in the biological system. The chemical reactions which are catalyzed by these enzymes are studied under the enzyme kinetics. The reaction rate is measured based on the rate at which the substrate of the enzymes combines with the enzyme and forms the products. 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 concentration of S where the velocity at maximum is half. V_max is the maximum velocity with which the enzyme catalyzes the reaction.

$\text{The rate of enzyme reaction }\left(\text{V}\right)\text{ =}\frac{{\text{V}}_{\text{max}}\left[\text{S}\right]}{\left({\text{K}}_{\text{M}}\text{+}\left[\text{S}\right]\right)}$