Calculate the physiological free energy for the substrate level generation of ATP from PEPcatalyzed by the enzyme Pyruvate Kinase:Phosphoenolpyruvate + ADP --> Pyruvate + ATPat 37C in a red blood cell where {PEP]=4.7mM. [pyruvate]=1.0mM. [ADP] = 0.73mM and[ATP] = 2.6 mMThe standard free energies of hydrolysis are:PEP--> pyruvate +Pi: -61.9 kJ/molATP --> ADP+ Pi: -30.5 kJ/moleReport to 1 decimal as kJ/mol

Step 1: Calculate the standard free energy change (ΔG′∘) ΔG′∘ = ΔGPEP→Pyruvate - ΔGATP→ADPΔG′∘ =…

Answered: Calculate the physiological free energy…

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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(b) the activity of the malate-aspartate shuttle (MAS) system of isolated rat brain mitochondria suspended in an isotonic me- dium buffered to pH 7.4. Diagram A illustrates NADH fluo- rescence emission upon addition of Glutamate in the ab- sence and presence of Aspartate. Diagram B illustrates sim- ilarly NADH fluorescence emission upon addition of Gluta- mate in the presence of Aspartate followed by additions of submicromolar concentrations of Ca2+. As is well estab- lished, the MAS in brain, skeletal muscle, and cardiac mus- Diagrams A and B on the right show changes in Glu A Glu В -No Asp + 0 +0.12 -0.48 + 16 0.81 +1.8 ++ Asp 10 min 2 min cle mitochondria is activated by cytosolic concentrations of Ca2* < 3 µM. To simulate the cytosolic part of the MAS, the following reagents were added to the medium: 4 units/ml glutamate-oxaloacetate transaminase, 6 units/ml malate dehydrogenase, 66 µM NADH, 5 mM aspartate, 5 mM malate, 0.5 mM ADP, 200 nM ruthenium red (to block the mitochondrial…
Give only typing answer with explanation and conclusion
Calculate what the intracellular glucose concentration should be if to transport glucose in active form from the external medium (c1 = 5 mM) at 37 ºC, a energy input of + 2970 J / mol.
Calcium is an important regulator of the citric acid cycle. Calcium is transported across the mitochondrial inner membrane by a Ca²- 2+ uniporter that is driven by the negative potential inside the matrix. Part A Assuming a membrane potential across the inner membrane of 172 mV (inside negative), calculate the ratio of the [Ca2+] in the matrix to that in the cytoplasm ([Ca2+]m/[Ca²+]c) that would exist at equilibrium (i.e., AG = 0). Express your answer using two significant figures. [Ca2+]m [Ca2+] = ΤΟ ΑΣΦ Submit Request Answer Part B ? Cytoplasmic [Ca2+] is on the order of 10-7 M in a healthy cell. Based on your answer in Part A, calculate the [Ca2+] that would exist in the matrix at equilibrium. Express your answer to two significant figures and include the appropriate units. ☐ μÅ ? Value Units
Aconitase catalyzes the conversion of Citrate to Isocitrate in the TCA cycle. The standard free energy change (AG°) for this reaction is +6.7 kJ/mol. The observed free energy change (AG) for the reaction in pig heart mitochondria is +0.8 kJ/mol. The ratio of [isocitrate]/[citrate] in these mitochondria is: Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a 10 b. 1 100 0.01 e f 0.33 0.10 h 0.25 i 2
what is the Vmax and Km of the enzyme in the reaction asap please.
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…
Please answer both parts, i and ii
Calculate the ΔG for Malate dehydrogenase reaction of CAC if the concentration of oxaloacetate is 1x 10-8 M, malate is 0.2 mM, NAD+ is 10 mM and NADH is 0.1 mM in rat liver mitochondria. ΔGo’ for this reaction is 30 kJ/mole. Please write the units of the final answer and the formula you are using to solve. R = 0.008314kJ/K*mol, T = 298K
Show summary computation in a table Net ATP yield for complete oxidation of 1 mol of mannose to CO2 and H2O (using both Malate-Aspartate and Glycerol-3-Phosphate Shuttles)

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