I need help anwsering all the following questions thankyou! QUESTION 11NADH can act as an inhibitor of isocitrate dehydrogenase and a-ketoglutarate dehydrogenase. This is anexample of:Negative allosteric regulationFeedback inhibitionFeed-forward activationProduct inhibitionQUESTION 12When the flux of the citric acid cycle is low, Acetyl-CoA accumulates. The high levels of Acetyl-CoA activatepyruvate carboxylase, which synthesizes oxaloacetate. This is an example of:a fermentation reactionsubstrate level phosphorylationan anaplerotic reactiona cataplerotic reactionQUESTION 13How does insulin influence glucose metabolism?O Leads to dephosphorylation of the PFK2/FBPase2 enzymeActivates to phosphorolysis of glycogenLeads to dephosphorylation of PFK1Leads to activation of FBPase1QUESTION 1431. Which of these substances from the Electron Transport Chain has the highest standard reduction potential (e°)?O2QH2NADHcytochrome cQUESTION 15Upon addition of Molecule X to actively respiring mitochondria, the QH2/Q ratio increased (higher levels of QH2compared to Q). Based on this observation: which component of the Electron Transport Chain is becominginhibited by Molecule X?O Complex IComplex IIComplex IVComplex III0000000 o QUESTION 7The table below summarizes the kinetic parameters for the phosphorylation of various substrates by anucleoside monophosphate kinase. Question: With which of these substrates is the nucleoside monophosphatekinase the most efficient?Substrate KM (mM)kcat (s-)keat/KM (M-'s-') K¡ (mM)D-dTMPD-dUMPL-dTMPL-dUMP1.5 x 10° (100“)2.8 x 10* (18)0.34 +0.03 900 (0.7)0.13+0.01 60 (0.04)0.020 +0.0053.0+0.12.6+0.90.17+0.010.38 +0.072.3+0.24.8 +0.65+1O D-DUMPL-DTMPD-dTMPO L-DUMPWhich of these metabolic reactions cannot be catalyzed by the same enzyme in the reverse direction?OC+D+EAG = +30.8 kJ/molOD EA+B>CAG = -1.0 kJ/molAG = +8 kJ/molAG = -25 kJ/mol%3DO ABQUESTION 10Choose the most accurate statement regarding the thermodynamics of metabolicreactions:O A reaction will take place under cellular conditions as longs as the concentrationof products is greater than that of the reactants.O The actual free energy change (AG) determines whether a reaction will takeplace under cellular conditions.The standard free energy change (AG") determines whether a reaction will takeplace under cellular conditions.O The membrane potential of a cell will determine whether a reaction will takeplace under cellular conditions.

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Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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QUESTION 22 When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Allosteric activation Zymogen activation Covalent modification Competitive inhibition Allosteric inhibition
Question:- The enzyme aromatase is found in the cytoplasm of some cells and converts testosterone to estrogen. You decide to test aromatase from a particular cell, and oops, your lab partner admits he drastically increased the pH in all the test tubes. Which of the following is a likely result? a. The enzyme will be denatured and the substrate will not bind to the active site. b. The enzyme will convert testosterone to estrogen at a faster rate. c. The mistake will have no effect on the experiment, because enzymes are not sensitive to pH. d. The free energy will be lowered and the reaction will not proceed spontaneously.
Question: A. To explore the consequences of coupling ATP hydrolysis under physiological conditions to a thermodynamically unfavorable biochemical reaction, consider the hypothetical transformation X⟶Y, for which Δ?′°=20.0 kJ/mol. What is the ratio of [Y]/[X][Y]/[X] at equilibrium? B. Suppose XX and YY participate in a sequence of reactions during which ATP is hydrolyzed to ADP and Pi. The overall reaction is X+ATP+H2O⟶Y+ADP+Pi Calculate [Y]/[X] for this reaction at equilibrium. Assume that the temperature is 25.0 °C and the equilibrium concentrations of ATP, ADP, and Pi are 1.00 M each. C. We know that [ATP], [ADP], and [Pi] are not 1.00 M under physiological conditions. Calculate [Y]/[X] for the ATP‑coupled reaction when the values of [ATP], [ADP], and [Pi] are those found in rat myocytes. Metabolite Concentration in rat myocytes (M) ATP 8.05x10-3 ADP 0.93x10-3 Pi 8.05x10-3
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QUESTION NO. 1Targeting a protein to be degraded within proteasomes usually requires ubiquitin. In the function of ubiquitin all of the following are true except: A. ATP is required for activation of ubiquicin. B. a peptide bond forms between the carboxyl terminal of ubiquitin and an ε-amino group of a lysine . C. linkage of a protein to ubiquitin does not always mark it for degradation. D. the N-terminal amino acid is one determinant of selection for degradation. E. ATP is required by the enzyme that transfers the ubiquitin to the protein to be degraded QUESTION NO. 2Much of procollagen formation occurs in the endoplasmic reticulum and Golgi apparatus which requires signal peptide. All of the following statements about targeting a protein for the ER are true except. A. signal peptide usually has a positively charged N-terminus and a stretch of hydrophobic amino acids. B. signal peptide emerging from a free ribosome binds signal recognition…
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Question 1: When the CAC is run in reverse by microorganisms that use it to fix carbon, the citrate synthase reaction is different and is catalyzed by an enzyme called ATP-citrate lyase. Write the reaction catalyzed by ATP-citrate lyase, then briefly (in one sentence) explain why the use of different chemistry (different from the ‘normal’ direction) makes sense here.
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NADH can act as an inhibitor of isocitrate dehydrogenase and a-ketoglutarate dehydrogenase. This is an example of: