Biology (MindTap Course List)
11th Edition
ISBN: 9781337392938
Author: Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Question
Chapter 7.4, Problem 1C
Summary Introduction
To write: Simple reactions illustrating the conversion of Substance X to Substance Y, which is an endergonic reaction and that can be driven if coupled to the hydrolysis of adenosine triphosphate (ATP).
Introduction: Both exergonic and endergonic reactions are type of
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Ethylene glycol (HO−CH2−CH2−OH) is a major component of antifreeze. In the body, it is first converted to HOOC−CHO (oxoethanoic acid) and then to HOOC−COOH (oxalic acid), which is toxic.
What class of enzyme catalyzes both of the reactions of ethylene glycol?
The treatment for the ingestion of ethylene glycol is an intravenous solution of ethanol. How might this help prevent toxic levels of oxalic acid in the body?
Sodium fluoroacetate (FH2CCOO- Na+) is highly toxic. Patients with fluoroacetate poisoning accumulate citrate and fluorocitrate in their cells. Which enzyme is inhibited by fluoroacetate for this to occur? Explain.
Consider the reaction:
H O
C—C—C—SCOA
H₂C(CH₂)C=
CO
H
H₂C-(CH₂)
What kind of reaction is being performed here?
b. What enzyme performs this reaction?
OH H O
O=C
-C—C—C—SCOA
H H
c. What cofactors, if any, are required for this reaction?
Chapter 7 Solutions
Biology (MindTap Course List)
Ch. 7.1 - Define energy, emphasizing how it is related to...Ch. 7.1 - Use examples to contrast potential energy and...Ch. 7.1 - Prob. 1CCh. 7.2 - Prob. 3LOCh. 7.2 - Prob. 1CCh. 7.2 - Life is sometimes described as a constant struggle...Ch. 7.3 - Prob. 4LOCh. 7.3 - Prob. 5LOCh. 7.3 - Prob. 6LOCh. 7.3 - Prob. 1C
Ch. 7.3 - Prob. 2CCh. 7.4 - Explain how the chemical structure of ATP allows...Ch. 7.4 - Prob. 1CCh. 7.4 - Prob. 2CCh. 7.5 - Relate the transfer of electrons (or hydrogen...Ch. 7.5 - PREDICT Which has the most energy, the oxidized...Ch. 7.6 - Explain how an enzyme lowers the required energy...Ch. 7.6 - Describe specific ways enzymes are regulated.Ch. 7.6 - Prob. 1CCh. 7.6 - How does the function of the active site of an...Ch. 7.6 - How are temperature and pH optima of an enzyme...Ch. 7.6 - Prob. 4CCh. 7 - Which of the following can do work in a cell? (a)...Ch. 7 - Prob. 2TYUCh. 7 - Prob. 3TYUCh. 7 - Test Your Understanding 4. Diffusion is an (a)...Ch. 7 - Prob. 5TYUCh. 7 - Prob. 6TYUCh. 7 - Prob. 7TYUCh. 7 - Test Your Understanding 8. Induced fit means that...Ch. 7 - Prob. 9TYUCh. 7 - Prob. 10TYUCh. 7 - PREDICT In the following reaction series, which...Ch. 7 - Test Your Understanding 12. EVOLUTION link All...Ch. 7 - EVOLUTION LINK Some have argued that evolution is...Ch. 7 - Prob. 14TYUCh. 7 - Prob. 15TYUCh. 7 - Prob. 16TYU
Knowledge Booster
Similar questions
- The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose 6-phosphate. After the reactants and products were mixed and allowed to reach equilibrium at 25°C, the concentration of glucose 1-phosphate was 4.5 mM and that of glucose 6-phosphate was 86 mM. Calculate Keq' and AG for this reaction. The reaction coordinate diagram for an enzyme-catalyzed reaction is shown below. How many transition states and intermediates are in the reaction? Is the reaction thermodynamically favorable? Which step is the rate-determining step of the reaction? G Reaction coordinatearrow_forwardEnzymes 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_forwardIn the reaction ATP + glucose → ADP + glucose-6-phosphate, ΔG° is -16.7 kJ/mol. Assume that both ATP and ADP have a concentration of 1 M and T = 25°C. What ratio of glucose-6- phosphate to glucose would allow the reverse reaction to occur?arrow_forward
- The protein catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide:2 H2O2 (aq) → 2 H2O (l) + O2 (g)and has a Michaelis-Menten constant of 25 × 10-3 mol·dm-3 and a turnover number of 4.0×107s-1.The total enzyme concentration is 0.016×10-6 mol·dm-3 and the initial substrate concentration is4.32×10-6 mol·dm-3 Calculate the maximum reaction rate (????) for this enzyme, and the initial rateof this reaction. Note that catalase has a single active site.arrow_forwardGiven the following information, calculate the catalytic efficiency of the enzyme. Step by step please [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμMarrow_forwardGiven the following enzyme catalyzed reaction, identify the class and subclass of the enzyme involved: NADH NAD* + H* C-O C-OT C=0 H-C-OH CH CH Class: Subclass:arrow_forward
- How does the rate of the forward reaction compare to the rate of the reverse reaction for an endergonic reaction? For an exergonic reaction? Explain.arrow_forwardA particular reaction has a ΔG‡ of 37.0 kJ mol-1. In the presence of an enzyme, the same reaction has a ΔG‡ of 5.70 kJ mol-1. Calculate the value of ΔΔG‡ in kJ mol-1.arrow_forwardIn covalent catalysis, either nucleophilic catalysis or electrophilic catalysis occurs. Do you agree or disagree with this statement? Explain.arrow_forward
- Why is the overall coupled reaction exergonic?arrow_forwardAmylose n + Water → Amylosen-1 + Glucose (See attached image of chemical reaction for the above) 1) If amylose and amylase are left together in solution in a test tube for a long period of time, what will be left in the test tube at the end? 2) In an experiment amylase activity is measured immediately and 10 minutes after addition to a solution of amylose. Assume 10 minutes is enough time for amylose to act on all available substrate molecules in the solution. a) What colour would you expect to observe if you added iodine at the 0 minute time point? b) What colour would you expect to observe if you added iodine at the 10 minute time point?arrow_forwardAn enzyme has a single active site at which it can bind and hydrolyze either X or Y; however, the enzyme cannot bind X and Y at the same time. Answer the following questions regarding the Km and Vmax of this enzyme. (a) Will the Km for X be affected if Y is present in the reaction mixture? Explain. (b) Will Vmax for X be affected if Y is present in the reaction mixture? Explain. (a) No, X competes with Y for binding, so the apparent Km for X will stay the same. (b) Yes, the Vmax for X will decrease in the presence of Y. (a) No, Y does not compete with X for binding, so the apparent Km for X will stay the same. (b) No, the Vmax for X will be unaffected by the presence of Y.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- Human Anatomy & Physiology (11th Edition)BiologyISBN:9780134580999Author:Elaine N. Marieb, Katja N. HoehnPublisher:PEARSONBiology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStaxAnatomy & PhysiologyBiologyISBN:9781259398629Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa StouterPublisher:Mcgraw Hill Education,
- Molecular Biology of the Cell (Sixth Edition)BiologyISBN:9780815344322Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter WalterPublisher:W. W. Norton & CompanyLaboratory Manual For Human Anatomy & PhysiologyBiologyISBN:9781260159363Author:Martin, Terry R., Prentice-craver, CynthiaPublisher:McGraw-Hill Publishing Co.Inquiry Into Life (16th Edition)BiologyISBN:9781260231700Author:Sylvia S. Mader, Michael WindelspechtPublisher:McGraw Hill Education
Human Anatomy & Physiology (11th Edition)
Biology
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:PEARSON
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax
Anatomy & Physiology
Biology
ISBN:9781259398629
Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter
Publisher:Mcgraw Hill Education,
Molecular Biology of the Cell (Sixth Edition)
Biology
ISBN:9780815344322
Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter
Publisher:W. W. Norton & Company
Laboratory Manual For Human Anatomy & Physiology
Biology
ISBN:9781260159363
Author:Martin, Terry R., Prentice-craver, Cynthia
Publisher:McGraw-Hill Publishing Co.
Inquiry Into Life (16th Edition)
Biology
ISBN:9781260231700
Author:Sylvia S. Mader, Michael Windelspecht
Publisher:McGraw Hill Education