11. Calculate the equilibrium constant for the hydrolysis of glucose-1-phosphate at25°CAG ° for the reaction,Glucose -1-phosphate+ water Glucose + Pi is - 20.9 KJ.mol-¹112. Calculate the Agº for the reactionPhosohoenolpuruvateADP + Pi =====Phosphoenolpyruvate + H₂O+ ADP ==== Puruvate + ATPATP + H₂0 AG° = 30.5 KJ.mol-¹13. Calculate the AG for the reaction0A + B ====Pyruvate + Pi AG° = -61.9 KJ.mol-¹C + D at 25°C When equilibrium concentrations are(A) = 10µM(B) = 15μM(C) = 3џM(D) = 5µM. Is the reaction exergonic and endergonic under standard conditions?14. For the reaction A---B at 298K, the change in enthalpy is -7KJ.mol-¹ and thechange in entropy is -25 J.K-¹.mol-¹¹. Is the reaction spontaneous? If not, thetemperature be increased or decreased to make the reaction spontaneous?15. A spherical bacterium with a diameter of 1μm contains 2 molecules of a particularprotein. What is the molar concentration of the particular protein?

In a general reaction such as: aA + bB ⇌ cC + dD At equilibrium (steady state), the rate of forward…

Answered: 11. Calculate the equilibrium constant…

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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Explain the difference between ΔG°’ and ΔG and calculate the free energy (delta G) of hydrolysis of ATP in a rat liver cell in which the ATP, ADP, and Pi concentrations are 3.4, 1.3, and 4.8 mM.
Calculate theequilibrium constant and thefree energy of (Mg)ATP hydrolysis in a closed system in which concentrations of ATP, ADP and Piare, respectively, 3.5, 1.0, and 5 mMand 25 degrees Celsius. Is the reaction spontaneous?R = 8.314 J/(deg Kelvin-mol).
What is the Vmax of an enzyme at 1 μM with -4G RT k = 6.2x 10¹2 s-1 (Ideal gas constant R = 8.314 J K-1 mol-1) cat 0.14 μM S-1 1.4 µM s-1 14 μM s-1 0.14 mM s-1 1.4 mM s-1 activation energy (AG) of 55000 J/mol at 298K?
9. TCA cycle and electromotive force-Consider the following reaction: malate + NAD 32>oxaloacetate + NADH The free energy for this reaction depends on the [NAD]/[NADH] ratio and the [malate]/[oxaloacetate] ratio, with AGO' = 30 kJ/mol, AG° is simply AG°at pH 7. a) Assuming that the [malate]/[oxaloacetate] ratio is fixed at 10, generate a plot of AG versus [NAD]/[NADH]. b) Assuming that the [malate]/[oxaloacetate] ratio is still fixed at 10, in which direction will this portion of the TCA cycle run for [NAD]/[NADH] = 1?10?100? c) For [NAD+] = 10 mM and [NADH] = 0.1 mM, and the [malate]/[oxaloacetate] ratio still fixed at 10, what is AG for the above reaction?
2.1 ANSWER THE TABLE
Free energy changes under intracellular conditions differ markedly from those determined under standard conditions. ΔG°′ = -32.2 kJ/mol for ATP hydrolysis to ADP and Pi. Calculate ΔG for ATP hydrolysis in a cell at 37 °C that contains [ATP] = 3 mM, [ADP] = 1 mM, and 3Pi4 = 1 mM.
Calculate the number of ATPATP generated from one saturated 1212‑carbon fatty acid. Assume that each NADHNADH molecule generates 2.5 ATP2.5 ATP and that each FADH2FADH2 molecule generates 1.5 ATP1.5 ATP .
Many years later, in 1989, Wild, et al. revisited the idea of allosteric control of ATCase by CTP. They noted that CTP did indeed inhibit ATCase, but that the inhibition was always incomplete, even at high concentrations of CTP. They hypothesized that perhaps CTP did not act alone, but in combination with some other nucleotide. They tested the activity of ATCase in the presence of several nucleotide combinations. The results are shown in Table 3. a. What combination gives the most effective inhibition? b. What is the physiological significance of this combination? c. Revise Figure 1 to include this new information. d. Redraw Figure 2 to include this new information. How does the combination compare with the values for the nucleotides alone? Table 3: Relative specific activities for combinations of nucleotide effectors. A value greater than one indicates stimulation, a value less than one indicates inhibition. Nucleotide Effector ATP CTP GTP UTP ATP/CTP ATP/GTP ATP/UTP CTP/GTP CTP/UTP…

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