SAPLINGPLUS F/BIOCHEM+ICLICKER REEF-CODE
SAPLINGPLUS F/BIOCHEM+ICLICKER REEF-CODE
9th Edition
ISBN: 9781319398583
Author: BERG
Publisher: MAC HIGHER
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Chapter 8, Problem 38P
Interpretation Introduction

(a)

Interpretation:

The enzyme that has the higher affinity for substrate should be determined.

Concept introduction:

Michaelis Menten model describes the kinetic properties of enzymes. Enzyme and substrate combines to form an enzyme-substrate complex and form a product or it can go back to dissociated enzyme and substrate.

E + Sk1k1 ES k2 E + P

The rate of formation of product V0 is given by Michaelis-Menten equation,

V0=Vmax[S][S]+KM

The reaction rate when the enzyme is fully saturated with substrate is said to be Vmax. KM is the Michaelis constant which is the substrate concentration at the half of the Vmax.

Interpretation Introduction

(b)

Interpretation:

The initial velocity of the reaction should be determined when catalyzed by the wild type enzyme at the 10 mM substrate concentration.

Concept introduction:

KM is the Michaelis constant which is the substrate concentration at the half of the Vmax.

Interpretation Introduction

(c)

Interpretation:

Enzyme that varies the equilibrium more in the product direction should be determined.

Concept introduction:

Enzymes act as catalysts which increase the rate of the reaction by lowering the activation energy. Most of the enzymes are proteins.

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