From data in the table, calculate the AG value for the reactions.ReactionAG' (kJ/mol)Phosphocreatine + H₂O →>> creatine + P-43.0ADP + Pi → ATP + H₂O+30.5Fructose +P → fructose 6-phosphate + H₂O+15.9Phosphocreatine + ADP creatine + ATPAG'OATP + fructose → ADP + fructose 6-phosphateAG'°kJ/molkJ/mol

1. Phosphocreatine + ADP → Creatine + ATPThis reaction can be obtained by combining:Phosphocreatine…

Answered: From data in the table, calculate the…

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter3: The Plasma Membrane And Membrane Potential

Section: Chapter Questions

Problem 1SQE: Using the Nernst equation, calculate the equilibrium potential for Ca2 and for C1 from the following...

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Similar questions

Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.
Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?
The Reactions and Meehanisms of the Leloir Pathway Write the reactions that permit galactose to be utilized in glycolysis. Write a suitable mechanism, tor one of these reactions.
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.
Figure 6.8 Look at each of the processes shown, and decide if it is endergonic or exergonic. In each case, does enthalpy increase or decrease, and does entropy increase or decrease?
The Catabolism of Uric Acid Write a balanced equation for the oxidation of uric acid to glyoxylic acid, CO2, and NH3, showing each step in the process and naming all of the enzymes involved.
Do you think that the Ea for ATP hydrolysis is relatively low or high? Explain your reasoning.
MATHEMATICAL What yield of ATP can be expected from complete oxidation of each of the following substrates by the reactions of glycolysis, the citric acid cycle, and oxidative phosphorylation? (a) Fructose-1,6-bisphosphate (b) Glucose (c) Phosphoenolpyruvate (d) Glyceraldehyde-3-phosphate (e) NADH (f) Pyruvate
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?
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.
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.

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