**Phosphoenolpyruvate (PEP) Conversion to Pyruvate: Thermodynamics**Phosphoenolpyruvate (PEP) is converted to pyruvate by the enzyme pyruvate kinase. The standard free energy change (∆G°') for this reaction is -31.4 kJ/mol.**Problem Statement:**After consuming a candy bar, Billy's cellular concentrations are as follows:- Pyruvate = 0.04 mM- PEP = 12 mM**Question:**What is the ∆G of this reaction at 37°C?**Answer Choices:**- A) -33.3 kJ/mol- B) +6.3 kJ/mol- C) -46.1 kJ/mol- D) -2.4 kJ/mol- E) -16.7 kJ/mol**Explanation:**To solve for the actual free energy change (∆G) of the reaction under non-standard conditions, you can use the equation:\[ \Delta G = \Delta G^\circ' + RT \ln(Q) \]where:- \( R \) is the gas constant (8.314 J/mol·K),- \( T \) is the temperature in Kelvin (310 K for 37°C),- \( Q \) is the reaction quotient \(\left(\frac{[\text{products}]}{[\text{reactants}]}\right)\).**Calculation Steps:**1. Determine the reaction quotient \( Q = \frac{[\text{pyruvate}]}{[\text{PEP}]} \).2. Substitute the values into the equation to find \(\Delta G\). **Note:**Detailed calculations should be performed to determine the exact ∆G value, exploring how shifts in concentration from standard conditions affect the energy of the reaction.

The standard free energy change (∆Gº') is the amount of energy released in of biochemical reaction…

Answered: Phosphoenolpyruvate (PEP) is converted…

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

See similar textbooks

Similar questions

The following two reactions are coupled in the last step of glycolysis (catalyzed by the enzyme pyruvate kinase). РЕР + Н.О € Руr + Pi ADP + Pi → ATP + H2O AG° = -14.8 kcal/mol AG° = +7.3 kcal/mol D) The steady-state concentrations of ATP, ADP, and pyruvate in human erythrocytes are 2.24 mM, 0.25 mM, and 0.051 mM, respectively. What would be the concentration of PEP in these cells if the coupled reaction was at equilibrium?
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
The standard Gibbs (free) energy of reaction (A,Gº') of the following reaction is equal to zero (at 25 °C and pH 7) pyruvate + aspartate Pyruvate, aspartate and L-alanine are mixed each at a concentration of 1 mM, without oxaloacetate. Calculate the molar concentrations of each compound when the reaction reaches equilibrium. oxaloacétate + L-alanine
What is the reduction potential (DE) for the reaction catalyzed by isocitrate dehydrogenase if the citric acid cycle is fluxing? To get the answer scored correctly: Please report the answer to three decimal places. Example: 0.123 or -0.111 Do not include units.
Calculate the free energy change for glucose entry into cells when the extracellular concentration is 4.5 mM and the intracellular concentration is 2.1 mM at 37oC. Express your answer in kJ/mol.
Consider the following equilibrium at 298 K. R=8.314 J/K-mol Acetyl-CoA + Oxaloacetate + H20 Citrate + COASH + H* Which one of the following is the correct value for K'eg ifAG" = -32.2 kJ/mol? O 1.11 0.987 1.01 x 10-13 13.0 9.92 x 1012 2480 4.42 x 105 2.27 x 10-6 1.01 -2480 2.56 -13.0 1.08 -0.0130 0.0130 0.926
The cytochromes are heme-containing proteins that function as electron carriers in the mitochondria. Calculate the difference in the reduction potential (AE°') and the change in the standard free energy (AG°) when the electron flow is from the carrier with the lower reduction potential to the higher. cytochrome c₁ (Fe³+) + e¯ = cytochrome c₁ (Fe2+) E°' = 0.22 V cytochrome c (Fe³+) + e¯ = cytochrome c (Fe²+) E°' = 0.254 V Calculate AE°' and AG°'. AE°' = AG°' = V kJ/mol
Consider the malate dehydrogenase reaction from the citric acid cycle. Given the listed concentrations, calculate the free energy change for this reaction at energy change for this reaction at 37.0 °C (310 K). AG' for the reaction is +29.7 kJ/mol. Assume that the reaction occurs at pH 7. [malate] 1.25 mM [oxaloacetate] = 0.290 mM [NAD+] = 430 mM [NADH] : = 170 mM AG : kJ-mol-1 * TOOLS x10
The AG of the reaction C6H12O6 + 60₂ --> 6CO₂ + 6H₂O is -686 kcal/mol glucose oxidized. The AG of the reaction ADP + P₁ --> ATP + H₂O is + 7.3 kcal/mol ATP synthesized. The oxidation of glucose can be coupled to the synthesis of ATP. If the coupling is 50% efficient, how many molecules of ATP can be synthesized per molecule of glucose oxidized? Round your answer to the nearest whole number.
If palmitic acid is subjected to complete combustion in a bomb calorimeter, one can calculate a standard free energy of combustion of 9788 kJ/mol. From the ATP yield of palmitate oxidation, what is the metabolic efficiency of the biological oxidation, in terms of kilojoules saved as ATP per kilojoule released? (Ignore the cost of fatty acid activation.)
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
Glyceraldehyde-3-phosphate (GAP) is converted to 1,3-bisphosphoglycerate (1,3-BPG) as shown. GAP + P + NAD+ 1,3-BPG + NADH Is this reaction spontaneous? How do you know? AG = 6.7 kJ mol-¹ The reaction shown above is coupled to the following reaction in which 1,3-BPG is converted to 3-phosphoglycerate (3-PG): GAP + P + NAD+ + ADP3-PG + NADH + ATP AG = -18.8 kJ mol-¹ 1,3-BPG+ADP3-PG+ATP Write the equation for the overall conversion of GAP to 3PG. Is the coupled reaction favorable? How do you know?

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS

Phosphoenolpyruvate (PEP) is converted to pyruvate by the enzyme pyruvate kinase. The standard free energy change (delta Gº') is -31.4 kJ/mol. After eating a candy bar, Billy's cellular concentrations are pyruva = 0.04 mM and PEP = 12 mM. What is the delta G of this reaction at 37 %