Prescott's Microbiology
10th Edition
ISBN: 9781259281594
Author: Joanne Willey, Linda Sherwood Adjunt Professor Lecturer, Christopher J. Woolverton Professor
Publisher: McGraw-Hill Education
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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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Discuss an enzyme that acts as a catalyst in a biological system. What reaction(s) does it catalyze? What kinds of problems arise if the enzyme isn't working properly? In what ways is the enzyme's activity regulated? Other interesting facts about the enzyme? Don't forget to cite your source(s).
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.
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:
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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- infarrow_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_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.”arrow_forward
- Enzymes 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_forwardConsider 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_forwardList the 6 major groups of enzymes giving an example of each in the form of an equation.arrow_forward
- Enzymes 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_forwardList three effects of macromolecular crowding on the properties of enzymes and the reactions they catalyze.arrow_forward
- A mother in the kitchen squeezes a small lemon onto a fruit mix to avoid browning. Explain the kitchen technique that the mother used in terms of the Polyphenoloxidase enzyme chemistry you learned from the experiment.arrow_forwardUsing an energy diagram, show why the lock-and-key model could lead to an inefficient enzyme mechanism. Hint: Remember that the distance to the transition state must be minimized for an enzyme to be an effective catalyst.arrow_forwardAn enzyme has a single active site at which it can bind and hydrolyze either X or Y but the enzyme cannot bind X and Y at the same time. Which of the following statements are TRUE? Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation. SHOW MORE The Km for X will be affected if Y is present in the reaction mixture. a Y is a competitive inhibitor of X. The Km for X will increase. d The Vmax for X will be affected if Y is present in the reaction mixture. pH dependence of Vmax reflects the ionization state of catalytic site residues. e Consider the following: X and Y are methanol (poisonous) and ethanol respectively. If the Km for X= 0.01 M and the Km f for Y = 0.001 M then 0.01 M Y is 10 times the concentration of Y required for 0.5 Vmax. Addition of an enzyme to a chemical reaction increases the ratio of products to reactants (Ken). A mutation in the active site of an enzyme resulting in a large increase in…arrow_forward
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