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 8.4, Problem 1R
Summary Introduction
To review:
The reason behind changes in the chemical composition of the enzyme only during catalysis and then retrieval of the same composition as before.
Introduction:
Enzymes make a reaction go faster. These molecules are either proteinaceous or nonproteinaceous. Most enzymes are proteins, and substrates are the molecules that the enzymes act on. In a reaction, the enzymes help turn reactants or the substrate into products by attaching the substrate to its active site. Every enzyme has a unique active site by the virtue of different amino acid combinations nesting within it. They will only bind to certain substrates and therefore they are highly “specific” in nature.
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Each type of enzyme contains a unique, intricately shapedbinding surface called an _____________________.
Allosteric activators block the active site, so the enzyme cannot bind
True
Or
False
Which type of enzyme (Table) catalyzes the following (given) reactions?
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Life: The Science of Biology
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- PREDICT In the following reaction series, which enzyme(s) is/are most likely to have an allosteric site to which the end product E binds? (a) enzyme 1 (b) enzyme 2 (c) enzyme 3 (d) enzyme 4 (e) enzymes 3 and 4arrow_forwardDetermine what class of enzyme catalyzes the following reactionarrow_forwardLead exerts its poisonous effect on enzymes by two mechanisms. Which mechanism is irreversible and why?arrow_forward
- Four important properties of enzymes are high catalytic rate,high degree of substrate specificity, negligible formation ofside products, and _____________________.arrow_forwardWhen chewing white bread, a sweet flavor generally begins to develop and the bread tastes sweeter the longer it is chewed, why does this happen and what enzyme is does this?arrow_forwardWhy does the specificity of the enzyme promote enzyme activity?arrow_forward
- Substrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a productive reaction to occur. Why, then, is some conformational flexibility also a requirement for catalysis?arrow_forwardIn covalent catalysis, either nucleophilic catalysis or electrophilic catalysis occurs. Do you agree or disagree with this statement? Explain.arrow_forwardDoes an enzyme-mediated reaction need the same, more, or less activation energy than the same reaction occurring without the presence of the enzyme? Explain why.arrow_forward
- Most efficient enzyme isarrow_forwardGiven the following data in enzyme-catalyzed reaction, what are the Vm, Km of with DEDS (presence of inhibitor) and without DEDS ( absence of inhibitor) and its type of inhibition.arrow_forwardWolfenden has stated that it is meaningless to distinguish between the “binding sites” and the “catalytic sites” of enzymes. Explain.arrow_forward
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