Biochemistry, The Molecular Basis of Life, 6th Edition
Biochemistry, The Molecular Basis of Life, 6th Edition
6th Edition
ISBN: 9780190259204
Author: Trudy McKee, James R. McKee
Publisher: Oxford University Press
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Chapter 6, Problem 63TQ
Summary Introduction

To analyze:

Calculation of kcat / Km, where kcat is the turnover number and Km is the Michaelis–Menten constant. Determine the alcoholeasily metabolized by alcohol dehydrogenase using the data given in the table:

Substrate Km ( μ M) kcat ( min1 )
Ethanol 960 480
1-butanol 440 450
1-hexanol 69 182
12-hydroxydodecanoate 50 146
All-trans-retinol 20 78
Benzyl alcohol 410 82
2-butanol 250000 285
cyclohexanol 31000 122

Introduction:

Km and kcat values are important to determine the activity of an enzyme and the rate of reaction. kcat refers to the number of the substratemolecules that areconverted into product, per unit time. Km isMichaelis–Mentenconstant. It represents the binding affinity of the substrate with the enzyme. The binding affinity of the enzymeis higher if the value of Km is lower. Collectively, Km and kcat are referred to as specificity constant.

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