SaplingPlus for Lehninger Principles of Biochemistry (Six-Month Access)
SaplingPlus for Lehninger Principles of Biochemistry (Six-Month Access)
7th Edition
ISBN: 9781319108236
Author: David L. Nelson, Michael M. Cox
Publisher: W. H. Freeman
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Chapter 6, Problem 17P
Summary Introduction

To determine: The turnover number (Kcat) of carbonic anhydrase in units of min-1.

Introduction:

Kcat is defined as a constant which is used to describe turnover rate of enzyme-substrate complex into product and enzyme. It is a turnover number of an enzyme which is used to indicate the conversion of maximum number of substrate into product per active site per unit time.

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Example 1: 1. Suppose an enzyme (MW = 5,000 g/mole) has a concentration of 0.05 mg/L. If the kcat is 1 x 10 s, what is the theoretical maximum reaction velocity for the enzyme? A) 1050 µM/s. B) 100 µM/s. C) 150 μM/s. D) 105 μM/s.
In 1956, E. P. Kennedy and S. B. Weiss published their study of membrane lipid phosphatidylcholine (lecithin) synthesis in rat liver. Their hypothesis was that phosphocholine joined with some cellular component to yield lecithin. In an earlier experiment, incubating 32 P-labeled phosphocholine at physiological temperature (37 °C) with broken cells from rat liver yielded labeled lecithin. This became their assay for the enzymes involved in lecithin synthesis. Determine the optimal pH for this enzyme and characterize the enzyme activity at different pH values. -O-P-O-CH2-CH₁₂-N(CH3)3 Phosphocholine H₂C-O-C-R HC-O-C-R2 + + + Cell fraction + ? HC-O-P-O-CH₁₂-CH₂-N(CH), O Phosphatidylcholine The researchers then centrifuged the broken cell preparation to separate the membranes from the soluble proteins. They tested three preparations: whole extract, membranes, and soluble proteins. Table 1 summarizes the results. Table 1: Cell fraction requirement for incorporation of 32p-phosphocholine into…
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