Complete the table by predicting the effect of each mutation on the pace of glycolysis in liver cells.MutationLoss of the allosteric site for ATP in phosphofructokinaseLoss of the binding site for citrate in phosphofructokinaseLoss of the phosphatase domain of the bifunctional enzyme that controls the level offructose 2,6-bisphosphateLoss of the binding site for fructose 1,6-bisphosphate in pyruvate kinasePace of glycolysisincreasedecreaseno change

PFK-1's loss of the ATP allosteric site:Normally, when energy levels are high, ATP suppresses PFK-1.…

Answered: Complete the table by predicting the…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 20P: Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy...

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Similar questions

Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
A Deficiency on 3-Phosphogtycerate Dehydrogenase Can Affect Amino Acid Metabolism Although serine is a nonessential amino acid, serine deficiency syndrome has been observed in humans. One such form of the syndrome is traceable to a deficiency in 3-phosphoglycerate dehydrogenase (see Figure 25.31). Individuals with this syndrome not only arc serine-deficient but also arc impaired in their ability to synthesize another common ammo acid, as well as a class of lipids. Describe why.
Complete oxidation of a 16-carbon fatty acid can yield 129 molecules of ATP Study Figure 19.2 and determine how many ATP molecules would be generated if a 16-carbon fatly acid were metabolized solely by the TCA cycle, in the form of S acetyl-CoA molecules.
Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.
Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.
Understanding the Mechanism of Hemolytic Anemia Genetic defects in glycolytic enzymes can have serious consequences for humans For example, defects in the gene for pyruvate kinase can result in a condition known as hemolytic anemia. Consult a reference to learn about hemolytic anemia, and discuss why such genetic defects lead to this condition.
Based on your knowledge of the structure of NAD+ and an assumption that coenzyme dissociation is the rate limiting step of the alcohol dehydrogenase mechanism, hypothesize why a N249W mutation at the coenzyme binding site would increase the rate of catalysis.
Radiotracer Labeling of Pyruvate from Glucose Determine the anticipated location in pyruvate of labeled carbons If glucose molecules labeled (in separate experiments.) with 14C at each position of (.tie carbon skeleton proceed through the glycolytic pathway.
Energetic of Fructose-1 ,6-bis P Hydrolysis (Integrates with Chapter 3.) The standard free energy change (G) for hydrolysis of fructose-1. 6-bisphosphate (FBP) to fructose-S-phosphate (F-6-P) and P: is -16.7 KJ/mol: FBP + H2O fructose-6-P + Pi The standard free energy change (G) for ATP hydrolysis is -30.5 KJ/mol: ATP + H2O ADP + Pj What is the standard free energy change for the phosphofructokinase reaction: ATP + fructose-6-P ADP + FBP b. What is the equilibrium constant for this reaction? c. Assuming the intracellular concentrations of [ATP] and (ADP] are maintained constant at 4 mM and 1.6 mM, respectively, in a rat liver cell, what will be the ratio of [FBP]/[fructose-6-P] when the phosphofructokinase reaction reaches equilibrium?
Using the answer code on the right, indicate which form of energy production is being described: 1. takes place in the mitochondrial matrix 2. produces H2O as a by-product 3. results in a rich yield of ATP 4. takes place in the cytosol 5. processes acetyl-CoA 6. takes place in the mitochondrial innermembrane cristae 7. converts glucose into two pyruvate molecules 8. uses molecular oxygen 9. accomplished by the electron transport system and ATP synthase (a) glycolysis (b) citric acid cycle (c) oxidative phosphorylation
Radiolabeling with 14C-Glutamate Describe the labeling pattern that would result from the introduction into the TCA cycle of glutamate labeled at Cy with 14C.

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