Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Question
Chapter 24, Problem 28P
Interpretation Introduction
Interpretation:
The rate of the enzyme in the presence of both the product in high number in case of cumulative feedback inhibition is to be calculated.
Concept introduction:
Biological reactions are catalyzed by biological catalyst known as enzymes. Enzymes do not take part in reaction rather it decreases the activation energy. In some reactions, the excess amount of product formation decreases the enzyme activity. This is known as feedback inhibition.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Need help.
Select all that apply.
What is true about the conformational aspects of coupling?
O The proton gradient is involved in the release of bound ATP from the synthase as a result of conformational change.
O The conformational states interconvert as a result of proton flux through the synthase.
There are two sites for substrate on the synthase and two possible conformational states: open (0) and tight-binding (T).
Dinitrophenol binds to and inhibits ATP synthase conformational changes, thus inhibiting ATP synthesis.
The Fo portion of ATP synthase acts as a rotary motor.
Crohn’s disease. Omega-3 fatty acids have been tested asa means to prevent relapse of Crohn’s disease. Two large,randomized, placebo-controlled studies have shown nosuch benefit from omega-3 fatty acids. Suppose you areasked to design an experiment to further study this claim.Imagine that you have collected data on Crohn’s relapsesin subjects who have used these omega-3 fatty acids and
similar subjects who have not used them and that you canmeasure incidences of relapse for these subjects. Statethe null and alternative hypotheses you would use in yourstudy.
Chapter 24 Solutions
Biochemistry
Ch. 24 - Prob. 1PCh. 24 - Prob. 2PCh. 24 - Prob. 3PCh. 24 - Prob. 4PCh. 24 - Prob. 5PCh. 24 - Prob. 6PCh. 24 - Prob. 7PCh. 24 - Prob. 8PCh. 24 - Prob. 9PCh. 24 - Prob. 10P
Ch. 24 - Prob. 11PCh. 24 - Prob. 12PCh. 24 - Prob. 13PCh. 24 - Prob. 14PCh. 24 - Prob. 15PCh. 24 - Prob. 16PCh. 24 - Prob. 17PCh. 24 - Prob. 18PCh. 24 - Prob. 19PCh. 24 - Prob. 20PCh. 24 - Prob. 21PCh. 24 - Prob. 22PCh. 24 - Prob. 23PCh. 24 - Prob. 24PCh. 24 - Prob. 25PCh. 24 - Prob. 26PCh. 24 - Prob. 27PCh. 24 - Prob. 28PCh. 24 - Prob. 29PCh. 24 - Prob. 30PCh. 24 - Prob. 31PCh. 24 - Prob. 32PCh. 24 - Prob. 33PCh. 24 - Prob. 34PCh. 24 - Prob. 35PCh. 24 - Prob. 36PCh. 24 - Prob. 37PCh. 24 - Prob. 38PCh. 24 - Prob. 39PCh. 24 - Prob. 40P
Knowledge Booster
Similar questions
- Inducers and Inhibitors of AEP. Short peptides such as legumain stabilization and activity modulation (LSAM) domain and αvβ3 integrin could enhance the activity of AEP. LSAM domain known as the prodomain of AEP blocks substrate binding before activation. This prodomain has a helical structure and two independent peptides. One is an activation peptide (AP, K287 to N323), and the other is a LSAM domain. LSAM domain remains even after AP is cleaved and released from protease at neutral pH via electrostatic interaction. AEP without LSAM domain has a lower melting temperature than AEP with LSAM domain [77, 117]. Another short peptide, αvβ3 integrin, can directly interact with AEP, and after forming a complex, the optimal pH for AEP activity is increased from 5.5 to 6.0. It indicates that αvβ3 binding could induce conformational stabilization of AEP accompanied by deprotonated C189. αvβ3 does not directly interact with the AEP active site; however, AEP docks to the αvβ3 RGD-binding site…arrow_forwardCalculation about delta standard G, delta H, detla S. Question attached as photo below. And my answer attempted. Need my answer verified and corrected if neccesary. Please let me know where I got wrong and what key ideas I had miss. Thanks.arrow_forwardMatch with the given reactionA. The reaction that is slowest in reacting with the enzymeB. The reaction that is fastest in reacting with the glucose oxidaseC. The reaction that is most fitted in the active site of the enzymearrow_forward
- disease. As such, a frontline treatment for Type 2 diabetes is the drug metformin, which acts indirectly to inhibit gluconeogenesis in the liver. You are a research biochemist who would like to develop new drugs that act to directly inhibit gluconeogenesis. You have just gained access to a library of thousands of small molecules of unknown activity, and you would like to identify lead compounds that have specific inhibitory activity against steps in the gluconeogenesis pathway. (a) into PEP in order to screen for inhibitors of enzymes specific to gluconeogenesis. Which enzymes do you need to purify, what cofactors and allosteric effectors do they require, and which reactants do you need to add to reconstitute the reactions for the first bypass? Which intermediates and products are generated? Your first approach is to reconstitute the initial set of bypass reactions that convert pyruvate (b) vitro reconstitution? What additional steps and enzymes are required in liver cells but are…arrow_forwardLess energetic electrons. Why are electrons carried by FADH2FADH2 not as energy rich as those carried by NADH? What is the consequence of this difference?arrow_forwardRequired partner. Aminotransferases require which of the following cofactors: a. NAD+/NADP+NAD+/NADP+ b. Pyridoxal phosphate c. Thiamine pyrophosphate d. Biopterinarrow_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