Prescott's Microbiology
10th Edition
ISBN: 9781259662621
Author: WILLEY
Publisher: MCG
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Textbook Question
Chapter 10.6, Problem 2RIA
Illustrate the effect enzymes have on the activation energy of the reactions they catalyze. What is a transition state complex? Use your drawing to explain why enzymes do not change the equilibria of the reactions they catalyze.
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Students have asked these similar questions
Consider the analogy of the jiggling box containing coins that was described on page 85. The reaction, the flipping of coins that either face heads up (h) or tails up (T), is described by the equation h ↔ T, where the rate of the forward reaction equals the rate of the reverse reaction.a. What are ΔG and ΔG° in this analogy? b. What corresponds to the temperature at which the reaction proceeds? What corresponds to the activation energy of the reaction? assume you have an “enzyme,” called jigglase, which catalyzes this reaction. What would the effect of jigglase be and what, mechanically, might jigglase do in this analogy?
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the
statements that are true.
Without
enzyme
With
enzyme
A+B
Time
AB
O a. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction
O b. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the
uncatalyzed reaction
O c. The enzyme stabilizes the transition state for the reaction
Od. The reaction is exergonic
е.
The reaction is now spontaneous due to the addition of enzyme
Released Energy
When biological enzymes are heated, they lose their catalytic activity. The change that occurs is an ENDOTHERMIC and SPONTANEOUS process.
Based on the given information, what is the sign of Δ˚G?
Based on the given information, what is the sign of Δ˚H?
Is the structure of the original enzyme MORE or LESS ordered than the new form? Explain your answer.
Chapter 10 Solutions
Prescott's Microbiology
Ch. 10.1 - Figure 10.2 The Relationship of G to the...Ch. 10.1 - What kinds of work are carried out in a cell?...Ch. 10.1 - What is thermodynamics? Summarize the first and...Ch. 10.1 - Define entropy and enthalpy. Do living cells...Ch. 10.1 - Prob. 4RIACh. 10.1 - Prob. 5RIACh. 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. 2MI
Ch. 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 - What is an apoenzyme? A holoenzyme? What are the...Ch. 10.6 - Illustrate the effect enzymes have on the...Ch. 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 - Figure 10.21 Feedback Inhibition. Feedback...Ch. 10.7 - Briefly describe the three ways a metabolic...Ch. 10.7 - Define the terms metabolic channeling and...Ch. 10.7 - Define allosteric enzyme and allosteric effector.Ch. 10.7 - Prob. 4RIACh. 10.7 - Prob. 5RIACh. 10.7 - What is the significance of the fact that...Ch. 10 - Examine the structures of macromolecules in...Ch. 10 - Most enzymes do not operate at their biochemical...Ch. 10 - Examine the branched pathway shown here for the...Ch. 10 - Prob. 4CHI
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- Enzymes are biological catalysts that fulfill the following general reaction mechanism: E+S [ES] [EP] E + P Where E is enzyme, S is substrate, and P is product. Briefly describe how an enzyme is able to speed of the rate of a reaction:arrow_forwardEnzymes are catalytic proteins or RNA molecules that accelerate chemical reactions. Substrates are the molecules that are acted upon by enzymes and are converted into products through the binding of substrates to an enzyme’s active site. Figure 1 below shows a protein enzyme’s active site and four potential protein substrates. Table 1 indicates the different chemical properties at several locations in a hypothetical enzyme’s active site, and Table 2 indicates the different chemical properties at several locations in the potential substrates. Locations labeled “A” in the enzyme’s active site and on the substrate will attempt to interact, as will locations that are labeled “B” and “C. Based on Figure 1, explain whether the enzyme is more likely to bind with substrate 2 or substrate 4.arrow_forwardEnzymes are catalytic proteins or RNA molecules that accelerate chemical reactions. Substrates are the molecules that are acted upon by enzymes and are converted into products through the binding of substrates to an enzyme’s active site. Figure 1 below shows a protein enzyme’s active site and four potential protein substrates. Table 1 indicates the different chemical properties at several locations in a hypothetical enzyme’s active site, and Table 2 indicates the different chemical properties at several locations in the potential substrates. Locations labeled “A” in the enzyme’s active site and on the substrate will attempt to interact, as will locations that are labeled “B” and “C. Describe, in terms of energy, how enzymes catalyze chemical reactions.arrow_forward
- Consider the three-dimensional model of the tertiary structure of an enzyme below. Amino acids involved in binding are shaded blue, and amino acids involved in catalysis are shaded red.arrow_forwardWould you expect an “enzyme” designed to bind its target substrate as tightly as it binds the reaction transition state to show a rate enhancement over the uncatalyzed reaction? In other words, would such protein be a catalyst? Use a reaction energy diagram to explain why or why not.arrow_forwardList the 6 major groups of enzymes giving an example of each in the form of an equation.arrow_forward
- If you wanted to improve the catalytic efficiency of an enzyme, what changes might you make to the enzyme and why? Consider what factors affect catalysis. You can suggest a change in the environment or a change in the protein itself.arrow_forwardEnzymes can be regulated in a many different ways. Covalent modification is one way. Here, the functional groups are attached to or removed from the enzyme. A phosphate group is an example of a functional group that can be added to an enzyme. Depending on the enzyme, addition of a phosphate group can either increase or decrease an enzyme's activity. Evaluate the following names and identify the general name of an enzyme that functions to add phosphate groups to its substrate? A. isomerase B. phosphatase C. kinase D. ligasearrow_forwardEnzymes are important molecules in biochemistry that catalyze reactions. The energy diagram illustrates the difference between a catalyzed reaction and an uncatalyzed reaction. Label the energy diagram. Answer Bank activation energy reactants (substrate) free energy reaction progress transition state uncatalyzed reaction catalyzed reaction AG for reaction productsarrow_forward
- List three effects of macromolecular crowding on the properties of enzymes and the reactions they catalyze.arrow_forwardWhat are enzymes? What distinguishes enzymes from regular chemical catalysts? On the specificity of enzyme action, please comment. Which factor accounts for their specificity the most? Describe the enzyme catalysis mechanism.arrow_forwardWhich of the following is not a mechanism that enzymes use to lower the activation energy of a reaction?arrow_forward
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