Prescott's Microbiology
11th Edition
ISBN: 9781260211887
Author: WILLEY, Sandman, Wood
Publisher: McGraw Hill
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Textbook Question
Chapter 10.6, Problem 1MI
Will an enzyme with a relatively high Km have a high or low affinity for its substrate? Explain.
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Other things being equal, what is a potential disadvantage of an enzyme having a very high affinity for its substrate?
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Chapter 10 Solutions
Prescott's Microbiology
Ch. 10.1 - Figure 10.2 The Relationship of G to the...Ch. 10.1 - Prob. 1CCCh. 10.1 - Prob. 2CCCh. 10.1 - Prob. 3CCCh. 10.1 - Prob. 4CCCh. 10.2 - Why is ATP called a high-energy molecule? How is...Ch. 10.2 - Describe the energy cycle and ATPs role in it....Ch. 10.3 - Prob. 1MICh. 10.3 - Prob. 2MICh. 10.4 - Figure 10.6 Electron Movement and Reduction...
Ch. 10.4 - How is the direction of electron flow between...Ch. 10.4 - When electrons flow from the NAD+/NADH conjugate...Ch. 10.4 - Which among the following would be the best...Ch. 10.4 - In general terms, how is G related to E0? What is...Ch. 10.4 - Name and briefly describe the major electron...Ch. 10.6 - Will an enzyme with a relatively high Km have a...Ch. 10.6 - Prob. 2MICh. 10.6 - Prob. 1CCCh. 10.6 - Prob. 2CCCh. 10.6 - How does enzyme activity change with substrate...Ch. 10.6 - What special properties might an enzyme isolated...Ch. 10.6 - What are competitive and noncompetitive...Ch. 10.6 - How are enzymes and ribozymes similar? How do they...Ch. 10.7 - Figure 10.19 Allosteric Regulation. The structure...Ch. 10.7 - Prob. 2MICh. 10.7 - Define the terms metabolic channeling and...Ch. 10.7 - Define allosteric enzyme and allosteric effector.Ch. 10.7 - Prob. 3CCCh. 10.7 - Prob. 4CCCh. 10.7 - Prob. 5CCCh. 10 - Prob. 1RCCh. 10 - Prob. 2RCCh. 10 - Prob. 3RCCh. 10 - Examine the structures of macromolecules in...Ch. 10 - Examine the branched pathway shown here for the...Ch. 10 - Prob. 3AL
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- Under what conditions can we assume that KM indicates the binding affinity between substrate and enzyme?arrow_forwardWhy does the enzyme activity eventually fall as more PALA is present?arrow_forwardUnder what circumstances may we believe that KM represents the substrate-enzyme binding affinity?arrow_forward
- Why do we not determine the initial reaction rate when the enzyme is saturated with substrate?arrow_forwardIn concerted model, all subunits in the enzyme are either in the low affinity or high affinity forms.arrow_forwardAn enzyme with a Km of 3X10-5 M has a lower affinity for its substrate than an enzyme with a Km of 2x10-6 M. Is this true or false?arrow_forward
- Does 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_forwardWhy is an enzyme highly specific for the type of reaction it will promote?arrow_forwardWhat happens to a denatured enzyme regarding its functionality? How can that result be explained with the help of the lock and key model?arrow_forward
- What is the difference between enzyme limited and a substrate limited reaction?arrow_forwardWould you expect an irreversible inhibitor of an enzyme to be bound by covalent or by noncovalent interactions? Why?arrow_forwardWhy is ATP alone not an effective allosteric regulator of enzyme activity?arrow_forward
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