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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The AG" of hydrolysis (ATP + H2O --> ADP + Pi) is -31.0 kJ/mol. Answer the following questions assuming that the steady-state concentrations in the cell are as indicated below. (Note: Steady-state refers to a non-equilibrium situation that exists due to a balance between reactions that supply and remove these substances.) [ADP] = 0.40 mM, [ATP] = 4.0 mM, and [Pi] = 40.0 mM a) Calculate the equilibrium constant for this reaction. b) What would the AG' for ATP hydrolysis be in the cell? c) Is this reaction at equilibrium in the cell? Briefly explain your answer.
Consider the reaction: phosphoglucoisomerase Glucose 6-phosphate: glucose 1-phosphate After reactant and product were mixed and allowed to reach at 25 °C, the concentration of each compound at equilibrium was measured: [Glucose 1-phosphate] = 0.01 M [Glucose 6-phosphate] = 0.19 M Calculate Keq and AG°'. Код .0526 Incorrect Answer 7.30 AG°' kJ mol-1 Incorrect Answer
The phosphorylation of glucose to glucose 6-phosphate is the initial step in the catabolism of glucose. The direct phosphorylation of glucose by P, is described by the equation Glucose + P → glucose 6-phosphate + H₂O AG' = 13.8 kJ/mol In principle, at least, one way to increase the concentration of glucose 6-phosphate (G6P) is to drive the equilibrium reaction to the right by increasing the intracellular concentrations of glucose and Pj. The maximum solubility of glucose is less than 1 M, and the normal physiological concentration of G6P is 250 μM. Assume a fixed concentration of P, at 4.8 mM. The calculated value of K'cq is 4.74 × 10-³ M-¹. Calculate the intracellular concentration of glucose when the equilibrium concentration of glucose 6-phosphate is 250 μM, the normal physiological concentration. [glucose] = 10.99 Correct Answer Would increasing the concentration of glucose be a physiologically reasonable way to increase the concentration of G6P? No. Because the concentration of P,…
Assume that an enzyme-catalyzed reaction follows the scheme shown: E+S SES →E + P k₁ = 1 x 109/M-s k-1=2.5 x 10%/s k₂ = 3.4 x 107/s What is the dissociation constant for the enzyme-substrate, K,? What is the Michaelis constant, Km, for this enzyme? What is the turnover number, Keat, for this enzyme? What is the catalytic efficiency for the enzyme? If the initial Et concentration is 0.25mM, what is Vmax?
Using the Nernst equation, calculate the equilibrium potential for Ca2 and for C1 from the following sets of data: a. Given [ Ca2+ ]0=1mM,[ Ca2+ ]i=100nM, find Eca2+ b. Given [ Cl- ]0=110mM,[ Cl- ]i=100mM, find Ecl
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.

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