Life: The Science of Biology
Life: The Science of Biology
11th Edition
ISBN: 9781319010164
Author: David E. Sadava, David M. Hillis, H. Craig Heller, Sally D. Hacker
Publisher: W. H. Freeman
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Chapter 8.5, Problem 3R
Summary Introduction

To review:

The mechanism that can be used to investigate whether the enzyme catalase has a nonallosteric or the allosteric mechanism of action and whether pollutants that inhibit the catalase enzyme act as noncompetitive or competitive inhibitors.

Introduction:

An allosteric enzyme has a quaternary structure of the protein. The quaternary structure of the protein has many subunits that are attached to one another with the help of disulfide and other noncovalent forces of attraction. Since there are multiple subunits of proteins, each unit has many active sites. The active sites of the proteins are those at, which the substrates binding takes place. In a nonallosteric protein or enzyme, there is only one active site that binds to the substrate.

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Compare and contrast the enzymes catalase, superoxide dismutase, and superoxide reductase from the following points of view: substrates, oxygen products, organisms containing them, and their role in oxygen tolerance of the cell.
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6th Grade Science - Module 2: Physical & Chemical Properties; Author: iUniversity Prep;https://www.youtube.com/watch?v=4DONkU6c2Rs;License: Standard youtube license