2. The overall reaction for the activation of a fatty acid to fatty acyl-CoA, with concomitanthydrolysis of ATP to AMP, has a free energy change of about zero. The reaction isfavorable because of subsequent hydrolysis of pyrophosphate to orthophosphate (thereaction has a AG°' value of -19.2 kJ · mol-1). a. Write the equation for the coupledreaction and calculate AGº' (assume a temperature of 25°C). b. Calculate the equilibriumconstant for the reaction.

Fatty acid cannot enter mitochondria. To enter mitochondria, it must be activated by adding a CoA to…

Answered: 2. The overall reaction for the…

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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Consider the complete oxidation of one mole of simple TAG containing behenic acid residues (22:0). I. For one mole of the fatty acid residue, determine the following: c. ATP yield obtained from FADH2 coming from the complete β-oxidation of the fatty acid residue d. net ATP yield of ATP in the complete oxidation of the fatty acid residue
At what substrate concentration would an enzyme with a kcat of 33.0 s-1 and a Km of 0.0046 M operate at one-tenth of its maximum rate? Assume the enzyme obeys Michaeli s-Menten kinetics.
Given that the AG" values for the hydrolysis of glucose 1-phosphate and glucose 6-phosphate are approximately -21 kJ/mol and –14 kJ/mol, respectively, which statement is true regarding the isomerization shown? glucose 1-phosphate → glucose 6-phosphate O The reaction can likely proceed in either direction and will therefore depend on the concentrations of glucose 1-phosphate and glucose 6-phosphate. O Only the anabolic direction will occur because the free energy change is positive. O The reaction will proceed in both directions simultaneously. This reaction can only proceed in one direction and must be the rate limiting reaction for this point in metabolism.
23. Calculate the free energy of hydrolysis ATP in a rat liver cell in which the ATP, ADP, and Pi concentrations are 3.4, 1.3, and 4.8 mM, respectively. AG" for this hydrolysis -31.5 kJ/mol
11. Quantitative Relationships between Rate Constants to Calculate Km, Kinetic Efficiency (kcat/Km) and Vmax - II Triose phosphate isomerase catalyzes the conversion of glyceraldehyde-3-phosphate to dihydroxyacetone phosphate. Glyceraldehyde-3-P dihydroxyacetone-P The Km of this enzyme for its substrate glyceraldehyde-3-phosphate is 1.8 x 10-5 M When [glyceraldehydes-3-phosphate] = 30 μM, the rate of the reaction, v, was 82.5 μmol mL-1 s-1. a. What is Vmax for this enzyme? b. Assuming 3 nm/mL of enzyme was used in this experiment (E total = 3nm/mL) for this enzyme? c. What is the catalytic efficiency (kcat/km) for triose phosphate isomerase? d. Does this enzyme reach catalytic perfection?
The conversion of dihyroxyacetone phosphate to glyceraldehyde 3-phosphate, catalyzed by triose phosphate isomerase, has an equilibrium constant of Keq’ = 0.0475. Calculate the standard free-energy change for this reaction at 25ºC and pH 7.0.
The equilibrium constant for the hydrolysis of the peptide alanylglycine (Gly-Ala in the reaction from Part B) by a peptidase is K = 9.0 × 10² at 310 K. Calculate AG for this reaction. Express the Gibbs free energy to three significant figures. AG = Submit ΠΑΠΙ ΑΣΦ Request Answer ? kJ/mol Keq [Gly] [Ala] [Gly-Ala]
A) Calculate the Gibbs free energy change for the following reaction: Fructose diphosphate If the reaction is performed at 27°C and AH is 1,246 calories and AS is 4 calories/K. Is this a spontaneous or non-spontaneous reaction. Why? Is the reaction endergonic or exergonic? DHAP+ Glyceraldehyde phosphate
2.1
23. An important step in glycolysis is the formation of ATP and pyruvate from phosphoenol-pyruvate (PEP) and ADP. PEP ADP pyruvate+ATP The equilibrium constant (Keq) for this reaction is approximately 2.5x10°. Calculate standard free energy change (AG°') for this reaction. Show your work. onege b. Is the reaction exergonic or endergonic at standard conditions? If, at equilibrium, the concentrations of ADP and ATP are 0.2 mM and 2.0 mM, respectively, what is the equilibrium concentration ratio of [pyruvate] to [PEP]? Show your work. с.
ver is given. A +B C+ D 1) Calculate AG for the above react un and indicáte whether the reaction is favorable or unfavorable [A] = 0.9 M 20°C AG° = 4 KJ/mol %3D [B] = 15mM [C] = 4mM [D] = 3 M R= 8.314 J/moleK %3D %3D 4.7 and explain how you know.
Calculate AG for this reaction under the following conditions: 37°C, pH 7, [Pyruvate] = [CO₂] = 4.0 mM, [OAA] = 2.0 mM, [ATP] = 3.5 mM, [P;] = 5.0 mM, and [ADP] = 1.8 mM. Use 2 signficant figures. AG= i kJ.mol-1 Under these conditions, the reaction is (Tolerance is +/- 2%)

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