2 SEM CARDLESS ACC W/RAVEN TEXT
12th Edition
ISBN: 9781265810467
Author: Raven
Publisher: MCGRAW-HILL HIGHER EDUCATION
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Textbook Question
Chapter 6, Problem 1S
Examine the graph showing the
a. Describe what is happening to the enzyme at around 40°C.
b. Explain why the line touches the x-axis at approximately 20°C and 45°C.
c. Average body temperature for humans is 37°C. Suggest a reason why the temperature optimum of this enzyme is greater than 37°C.
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The FMO3 enzyme has an important physiological function in people. State the normal substrate of FMO3 in people and describe a genetic polymorphism that can reduce the activity of this enzyme. Describe the consequence to people with the reduced FMO3 activity. Give at least one reference from the primary literature (i.e. a scientific journal) to support your answer.
Consider these three sketches:
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what is A?
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3
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O (none of them)
0
0
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Chapter 6 Solutions
2 SEM CARDLESS ACC W/RAVEN TEXT
Ch. 6.1 - Prob. 1LOCh. 6.1 - Prob. 2LOCh. 6.1 - Describe the nature of redox reactions.Ch. 6.2 - Explain the laws of thermodynamics.Ch. 6.2 - Prob. 2LOCh. 6.2 - Contrast the course of a reaction with and without...Ch. 6.3 - Describe the role of ATP in short-term energy...Ch. 6.3 - Prob. 2LOCh. 6.4 - Discuss the specificity of enzymes.Ch. 6.4 - Explain how enzymes bind to their substrates.
Ch. 6.4 - Prob. 3LOCh. 6.5 - Prob. 1LOCh. 6.5 - Prob. 2LOCh. 6.5 - Prob. 3LOCh. 6 - Prob. 1DACh. 6 - A covalent bond between two atoms represents what...Ch. 6 - During a redox reaction the molecule that gains an...Ch. 6 - Prob. 3UCh. 6 - A spontaneous reaction is one in which a. the...Ch. 6 - Prob. 5UCh. 6 - Which of the following is NOT a properly of a...Ch. 6 - Where is the energy stored in a molecule of ATP?...Ch. 6 - Prob. 1ACh. 6 - Which of the following statements is NOT true...Ch. 6 - Prob. 3ACh. 6 - Prob. 4ACh. 6 - Enzymes have similar responses to both changes in...Ch. 6 - Prob. 6ACh. 6 - Examine the graph showing the rate of reaction...Ch. 6 - Phosphofructokinase functions to add a phosphate...
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- What are the correct terms that go with the definition?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_forwardCellular respiration is the primary process by which cells generate ATP.a. What is the balanced chemical reaction for cellular respiration? b. Describe how each of the reactants are utilized in this reaction, what product they are used to produce, and the steps in which they are used to form the products c. Why is the energy yield in this reaction different for eukaryotes and prokaryotes? Be specific. d. If a cell is deprived of oxygen, how does it modify the process of cellular respiration? Give the specific term for this alternate reaction.arrow_forward
- Which statement is/are TRUE about inhibitors? A. Mode of action of penicillin on bacteria is an example of irreversible inhibition. B. Increasing the substrate concentration does not affect competitive inhibitors C. Uncompetitive inhibitors bind only to the enzyme-substrate complex D. In the Lineweaver-Burke plot, the lines for enzymes in the presence and absence of noncompetitive inhibitor have different x-intercepts.arrow_forwardA high KM will result in an efficient enzyme. A. True B. False Specificity constant = Kcat/ KM kcat = Vmax [ET] A high Vmax will result in an efficient enzyme. A. True B. False Total enzyme concentration will have no effect on the efficiency of an enzyme catalysed reaction. A. True B. Falsearrow_forwardSuggest the possible class of enzyme (or name of enzyme) for each of theenzyme-catalyzed reactions below. Briefly explain your answer. d. ATP + L-tyrosine + tRNATyr → AMP + PPi + L-Tyrosyl-tRNATyrarrow_forward
- What is a limitation of the Michaelis-Menten kinetics? A. Enzymes have different binding sites which were not considered by the Michaelis-Menten assumption. B. Most enzymes are multimeric with many active sites. C. Variability in enzyme concentration due to synthesis and degradation by cells were not included in the Michaelis- Menten assumption. D. Enzymes have coenzymes that are involved in catalysis. E. Active sites can bind multiple substrates.arrow_forwardSuggest a reason why heating a solution containing an enzyme markedly decreases its activity. Why is the decrease of activity frequently much less when the solution contains high concentrations of the substrate?arrow_forwardDifferentiate the concerted model and sequential model by illustrating the difference in terms of R and T forms of the enzyme when a substrate is about to bind. Write a shortdescription for each.arrow_forward
- What are allosteric modulators? A. These are inhibitors that bind at sites other than the active site of enzymes resulting in the reduction of enzyme activities B. These are activators that bind at sites other than the active sites of enzymes resulting in enhanced enzyme activities. C. These are either inhibitors or activators that bind at the active site of enzymes. D. These are either inhibitors or activators that bind at sites other than the active sites of enzymes reducing or enhancing the latter's activities. E. These are small molecules that bind to an ES complex only.arrow_forwardA model is proposed to explain the reaction catalyzed by an enzyme. Experimentally obtained rate data fit the model to within experimental error. Do these findings prove the model?arrow_forwardWhich statements are true of an inhibitor that binds the active site of an enzyme? Select all that apply, there may be one correct answer or several. a These inhibitors are a kind of allosteric regulator that decreases enzyme activity. b Adding more substrate can reduce the effect of these inhibitors. c These inhibitors compete with the substrate for the active site of the enzyme. d These inhibitors increase the rate of enzyme activity. e These inhibitors function by changing the shape of the enzyme, stopping if from binding to substrate.arrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License