The table provides the standard reduction potential, E', for relevant half-cell reactions.Half-reactionE'° (V)Oxaloacetate² + 2H+ + 2e malate²--0.166Pyruvate + 2H+ + 2e → lactate-0.185Acetaldehyde + 2H+ + 2e¯ →→→ ethanol-0.197NAD+ + H+ + 2e--> NADH-0.320NADP+ + H+ + 2e →→ NADPHAcetoacetate + 2H+ + 2e¯--0.324B-hydroxybutyrate-0.346Which of the reactions listed would proceed in the direction shown, under standard conditions, in the presence of theappropriate enzymes?Malate + NAD+ oxaloacetate + NADH + H+Malate + pyruvate oxaloacetate + lactatePyruvate + NADH + H+ lactate + NAD+Pyruvate + p-hydroxybutyrate lactate + acetoacetateAcetaldehyde + succinate ethanol + fumerateAcetoacetate + NADH + H+ → B-hydroxybutyrate + NAD+

To determine which reactions proceed in the given direction under standard conditions, we use the…

Answered: The table provides the standard…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 13P

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Similar questions

Show the mechanism for the acid-catalyzed formation of an [α-1,6] glycosidic linkagebetween two molecules of α-D-glucopyranose. Please sketch the structure and use arrows showing electron flow!
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.
Extending the Mechanism of Methylmalonyl-CoA Mutase to Similar Reactions Based on the mechanism for the methylmalonyl-CoA mutase (see problem 14), write reasonable mechanisms for the following reactions shown.
Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.
Energetics of the Hexokinase Reaction The standard-state free energy change. Gfor the hexokinase reaction, is â€” 1 6.7 kJ/mol. Use the values in Table I to calculate the value of Gfor this reaction in the erythrocyte at 37Â°C.
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.
Understanding the Mechanism of the 3-ketosphinganine Synthase Reaction Write a reasonable mechanism for the 3-ketosphinganine synthase reaction, remembering that it is a pyridoxal phosphate-dependent reaction.
The Energy Cost of dTTP Synthesis (Integrates with Chapter 20.) Starting from HCO3, glutamine, aspartate, and ribosc-5-P, how many ATP equivalents are consumed in the synthesis of dTTP in a eukaryotic cell, assuming dihydroorotate oxidation is coupled to oxidative phosphorylation? How does this result compare with the ATP costs of purine nucleotide biosynthesis calculated in problem 2?
The Effect of lodoacetic Acid on the Glyceraldehyde-3-P Dehydrogenase Reaction (Integrates with Chapters 4 and 14.) How might iodoacetic acid affect the glyceraldehydes-3-phosphate dehydrogenase reaction in glycolysis? Justify your answer.
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?
Understanding the Mechanism of the -Ketoglutarate Dehydrogenase Reaction tshe first step of the -Ketoglutarate dehydrogenase reaction involves decarboxylation of the substrate and leaves a covalent TPP intermediate. Write a reasonable mechanism for this reaction.

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