Principles of Instrumental Analysis
Principles of Instrumental Analysis
7th Edition
ISBN: 9781305577213
Author: Douglas A. Skoog, F. James Holler, Stanley R. Crouch
Publisher: Cengage Learning
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Chapter 14, Problem 14.15QAP
Interpretation Introduction

Interpretation:

The concentration of a solution of tryptamine under given conditions should be determined.

Concept introduction:

The rate of the reaction is given by,

d[P]dt=k2[E]0[S]Km+[S]

[P] − product concentration

k2 − dissociation constant for enzyme substrate complex into products and free enzyme.

[E]0 − initial enzyme concentration

[S] − substrate concentration

Km − Michaelis constant

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7. A group of Colby students discovered a hydrolase that cleaves cellulose. After purifying the enzyme, an assay was performed by adding 0.1 μM of enzyme to the cellulose substrate concentrations shown below to characterize kinetic properties. [S] 2 x 10-6 M 4 x 10-6 1 x 10-5 2 x 10-5 4 x 10-5 1 x 10-4 2 x 10-3 1 x 10-² 4 x 10-² V (umol/min) 28 40 75 95 112 128 139 140 141 A. Use the data in the table above to estimate KM and Vmax for the enzyme. B. What is the keat of this enzyme? C. What is the catalytic efficiency of this enzyme?
An uncatalyzed reaction has an equilibrium constant, Keq, of 50. In the presence of an appropriate enzyme, the forward rate of the reaction increased by 20-fold. What is the equilibrium constant in the presence of the enzyme?
Consider the reaction. k₁ S P k₂ What effects are produced by an enzyme on the general reaction? AG for the reaction increases. The formation of the transition state is promoted. The reaction equilibrium is shifted toward the products. The concentration of the reactants is decreased. The activation energy for the reaction is lowered. The rate constant for the forward reaction (k₁1) increases.
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