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 46P
Interpretation Introduction

(a)

Interpretation:

V0 versus pH curve when the substrate concentration is much greater than the enzyme KM should be drawn.

Concept introduction:

KM is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower KM needs a higher concentration of substrate to achieve Vmax.

Interpretation Introduction

(b)

Interpretation:

V0 versus pH curve when the substrate concentration is much less than the enzyme KM should be drawn.

Concept introduction:

KM is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower KM needs a higher concentration of substrate to achieve Vmax.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

KM is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower KM needs a higher concentration of substrate to achieve Vmax.

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