Biochemistry: The Molecular Basis of Life
6th Edition
ISBN: 9780190209896
Author: Trudy McKee, James R. McKee
Publisher: Oxford University Press
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 6, Problem 13RQ
Summary Introduction
To review:
The models for the interactions of the allosteric enzymes. The application ofany of the models in studying the interaction of the oxygen molecules with hemoglobin.
Introduction:
In a biochemical reaction, there is a specific reaction between the enzyme and the substrate. The specific substrate of the enzyme can bind to the site of the catalytic activity. There are many sitesother than the catalytic site that are known as the allosteric sites, where any molecule or ligand other than the substrate can bind.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Explain how the position in the active site and function of the oxyanion hole of chymotrypsin supports the theory that enzymes preferentially bind the transition state of the reactions they catalyze
describe the mechanism of the phosphoglucoisomerase reaction
What kind of inhibitor is threo-sphingosine? Explain this type of inhibition.
Chapter 6 Solutions
Biochemistry: The Molecular Basis of Life
Ch. 6 - Prob. 1QCh. 6 - Prob. 2QCh. 6 - Prob. 3QCh. 6 - Prob. 4QCh. 6 - Prob. 5QCh. 6 - Prob. 6QCh. 6 - Prob. 7QCh. 6 - Prob. 8QCh. 6 - Prob. 9QCh. 6 - Prob. 1RQ
Ch. 6 - Prob. 2RQCh. 6 - Prob. 3RQCh. 6 - Prob. 4RQCh. 6 - Prob. 5RQCh. 6 - Prob. 6RQCh. 6 - Prob. 7RQCh. 6 - Prob. 8RQCh. 6 - Prob. 9RQCh. 6 - Prob. 10RQCh. 6 - Prob. 11RQCh. 6 - Prob. 12RQCh. 6 - Prob. 13RQCh. 6 - Prob. 14RQCh. 6 - Prob. 15RQCh. 6 - Prob. 16RQCh. 6 - Prob. 17RQCh. 6 - Prob. 18RQCh. 6 - Prob. 19RQCh. 6 - Prob. 20RQCh. 6 - Prob. 21RQCh. 6 - Prob. 22RQCh. 6 - Prob. 23RQCh. 6 - Prob. 24RQCh. 6 - Prob. 25RQCh. 6 - Prob. 26RQCh. 6 - Prob. 27RQCh. 6 - Prob. 28RQCh. 6 - Prob. 29RQCh. 6 - Prob. 30RQCh. 6 - Prob. 31RQCh. 6 - Prob. 32RQCh. 6 - Prob. 33RQCh. 6 - Prob. 34RQCh. 6 - Prob. 35RQCh. 6 - Prob. 36RQCh. 6 - Prob. 37RQCh. 6 - Prob. 38RQCh. 6 - Prob. 39RQCh. 6 - Prob. 40RQCh. 6 - Prob. 41RQCh. 6 - Prob. 42RQCh. 6 - Prob. 43FBCh. 6 - Prob. 44FBCh. 6 - Prob. 45FBCh. 6 - Prob. 46FBCh. 6 - Prob. 47FBCh. 6 - Prob. 48FBCh. 6 - Prob. 49FBCh. 6 - Prob. 50FBCh. 6 - Prob. 51FBCh. 6 - Prob. 52FBCh. 6 - Prob. 53SACh. 6 - Prob. 54SACh. 6 - Prob. 55SACh. 6 - Prob. 56SACh. 6 - Prob. 57SACh. 6 - Prob. 58TQCh. 6 - Prob. 59TQCh. 6 - Prob. 60TQCh. 6 - Prob. 61TQCh. 6 - Prob. 62TQCh. 6 - Prob. 63TQCh. 6 - Prob. 64TQCh. 6 - Prob. 65TQCh. 6 - Prob. 66TQCh. 6 - Prob. 67TQCh. 6 - Prob. 68TQCh. 6 - Prob. 69TQCh. 6 - Prob. 70TQCh. 6 - Prob. 71TQCh. 6 - Prob. 72TQCh. 6 - Prob. 73TQCh. 6 - Prob. 74TQCh. 6 - Prob. 75TQCh. 6 - Prob. 76TQCh. 6 - Prob. 77TQCh. 6 - Prob. 78TQCh. 6 - Prob. 79TQCh. 6 - Prob. 80TQCh. 6 - Prob. 81TQ
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Each of the following enzymes catalyzes what sort of reaction?citrate decarboxylase (a. citrate decarboxylase) (b. citrate decarboxyoxalate reductase (b)c. transaminase of serinearrow_forwardWhat is the catalytic triad on chymotrypsin? Detail its importance.arrow_forwardIdentify the two components of the nitrogenase complex and describe their specific tasks.arrow_forward
- Using lysozyme as an example, what can an enzyme’s structure reveal about its catalytic mechanism?arrow_forwardDescribe the products of the transketolase reaction when the substrates are a five-carbon aldose and a six-carbon ketose. Does it matter which of the substrates binds to the enzyme first?arrow_forwardWhy is the enzyme-catalyzed introduction of carbon–carbon double bonds into fatty acids called an electron transport system?arrow_forward
- A Proenzymes is inactive because it contain an additional polypeptide chain that masks(blocks) the active site of the enzyme?arrow_forwardName three weak forces by which the substrates bind in the active site of an enzyme.arrow_forwardHow many C02 molecules are produced from the complete oxidation of stearic acid through catabolic pathways? A. 14 B. 16 C. 18 D. 20arrow_forward
- How is a “committed step” defined in the context of a metabolic pathway and why are they important? Which steps and/or enzymes are involved in the committed steps in the Krebs Cycle? What are the possible implications of these steps were deregulated?arrow_forwardIdentify the enzyme that controls the oxidative phase of the pentose phosphate pathway.arrow_forwardIn a Lineweaver-Burk graph, the lines representing the uninhibited and inhibited enzyme catalyzed reaction meet each other on the x-axis. The type of inhibition which is occurring is: a) competitive b) noncompetitive c) uncompetitive d) allosteric CO2 exerts direct activity upon hemoglobin by: a) blocking oxygen from binding to the heme group b) displacing BPG from the central cavity c) oxidizing Fe+2 to Fe+3 which does not bind oxygen d) forming an N-terminal carbamate which favors the T-state The dominant motif found in hemoglobin and myoglobin is: a) helix-turn-helix b) twisted beta sheet c) beta barrel d) random coil Which of these is an ketohexose? a) fructose b) glucose c) ribose d) erythrose Which of these is a constitutional isomer of d-glucose? a) fructose b) galactose c) l-glucose d) ribose Which of these is an enantiomer of d-glucose? a) d-fructose b) d- galactose c) l-glucose d) d-ribose Which of these is a diastereomer of…arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON
Metabolic Pathways; Author: Wisc-Online;https://www.youtube.com/watch?v=m61bQYio9ys;License: Standard Youtube License