Prescott's Microbiology
11th Edition
ISBN: 9781260211887
Author: WILLEY, Sandman, Wood
Publisher: McGraw Hill
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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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An enzyme with a low Km is considered to have a higher affinity for the substrate. Provide
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Under what conditions can we assume that KM indicates the binding affinity between substrate and enzyme?
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 circumstances may we believe that KM represents the substrate-enzyme binding affinity?arrow_forwardHow does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction reaches a maximum value at high substrate?arrow_forwardWhy do we not determine the initial reaction rate when the enzyme is saturated with substrate?arrow_forward
- An 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_forwardConsider this intermediate in the derivation of the Michaelis-Menten equation. [E] [S] [ES| k-1 + kz km Assume that k is negligible compared to the other rate constants. If the k is very small, it suggests that the enzyme has a Select an option affinity for its substrate, while if the if the km is very large, it suggests that the enzyme has a Select an option. affinity for its substrate. Select an option Submit You have used 0 of high Sav low moderatearrow_forwardExplain how the following changes affect the rate of an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor: (a) increasing the substrate concentration at a constant inhibitor concentration, (b) decreasing the inhibitor concentration at a constant substrate concentration.arrow_forward
- Explain why the very tight binding of a substrate to an enzyme is not desirable for enzyme catalysis, whereas tight binding of the transition state is desirable.arrow_forwardEnzyme cofactors are usually inorganic ions that enhanceenzymatic activity by improving the “fit” between an enzymeand its substrate. True or false?arrow_forwardA generalized enzyme active site is shaped like a hemisphere with a radius of 45Å. The active site holds the following amino acids in a homeostatic solution (pH = 7.38): -HAVARILKHAVARILKHAVARILK- Assuming the charge is distributed uniformly along the hemisphere, determine the force at which this active site acts upon a single ATP molecule at the center of the hemisphere.arrow_forward
- In the absence of substrate, an allosteric enzyme that follows the concerted model has a T/R ratio of 300. Assume the ratio was inverted as a result of a mutation. What effect would this mutation have on the relationship between reaction rate and substrate concentration?arrow_forwardUsing lysozyme as an example, what can an enzyme’s structure reveal about its catalytic mechanism?arrow_forwardIn a uni uni enzyme reaction, what is the substrate concentration relative to Km when anenzyme operates at 0.95 * V. What about 0.99 * V?arrow_forward
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