Biochemistry (Looseleaf)
Biochemistry (Looseleaf)
9th Edition
ISBN: 9781319114800
Author: BERG
Publisher: MAC HIGHER
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Chapter 8, Problem 35P
Interpretation Introduction

Interpretation:

The effect of the mutation on the catalytic rate of an enzyme if the binding of the transition state is unaffected is to be stated.

Concept introduction:

The Michaelis-Menten equation relates the concentration of substrate with the velocity of the reaction. A constant which expresses the substrate’s concentration if the velocity of reaction equals half of the maximum velocity of the reaction is known as Michaelis-Menten constant. It is denoted by KM.

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Which type of enzyme catalyses the following reaction? oxidoreductase, transferase, hydrolase, lyase, isomerase, or ligase.
Which features of the curves in Figure 30-2 indicates that the enzyme is not consumed in the overall reaction? ES is lower in energy that E + S and EP is lower in energy than E + P. What does this tell you about the stability of ES versus E + S and EP versus E + P.
Looking at the figure 30-5 what intermolecular forces are present between the substrate and the enzyme and the substrate and cofactors.
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