Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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- 19. The AG, the standard free-energy change, for the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde 3-phosphate (GAP) is +7.55 kJ/mol. The reaction shown below is catalyzed by an enzyme called Triose Phosphate Isomerase (TPI). OH O OH DHAP OH TPI OH M+ OH GAP OH This reaction takes place in glycolysis. At equilibrium, the ratio of GAP to DHAP is 0.0475 at 25°C and pH 7.00. Equilibrium constant, Keq = 0.0475. A) Is the above reaction endergonic or exergonic (going from left to right) under the given experimental conditions? Why? B) Can the above reaction occur spontaneously under the given experimental conditions? Why or why not?arrow_forwardConsider the following equilibrium at 25ºC :Glucose-1-Phosphate Glucose-6-PhophateUsing the equilibrium concentrations of [Glucose-1-Phosphate] = 0.35 M and [Glucose-6-Phosphate] = 1.65 M, calculate BOTH K′eqand Gº′ for this reaction. Is this reaction exergonicor endergonic? R = 8.314 J/K·molarrow_forwardDetermine the yield in water for the complete oxidation of 1 molecule of a triglyceride containing 3, C16 fatty acids. Please do not show the (7-C)-6 formula. Can you please show me where each water molecule comes from that is considered for this calculation (TCA, ETC, B-oxidation and ATP synthase)? Thank you!arrow_forward
- Calculate the actual, physiological AG for the reaction Phosphocreatine + ADP = creatine + ATP at 37 °C, as it occurs in the cytosol of neurons, where [phosphocreatine] = 4.7 mM, [creatine] = 1.0 mM, [ADP] = 0.73 mM, and [ATP] = 2.6 mM. Standard Free Energies of Hydrolysis of Some Phosphorylated Compounds Phosphorylated compound AGʻ° (kJ/mol) phosphoenolpyruvate -61.9 phosphocreatine -43.0 ADP (→ AMP + P;) -32.8 ATP (→ ADP + P;) -30.5arrow_forwardCalculate Gibbs free energy for fructose+ATP= fructose-6-phosphate + ADParrow_forwardThe ΔG°′ for hydrolytically removing a phosphoryl group from ATP is about twice as large as the ΔG°′ for hydrolytically removing a phosphoryl group from AMP (−14 kJ · mol−1). Explain the discrepancy.arrow_forward
- [AktivGrid] Draw the product of the reaction of isocitrate catalyzed by isocitrate dehydrogenase in the TCA (citric acid) cycle. Provide the structure in the protonation state found in physiological conditions. rxn' F-C-H NAD+ isocitra te dehydro genase NADH, Dra H+, > Problem 5 of 12 Submit H Atoms, Bonds and Rings OH Charges CH2OH Drag To Pan CH2OH- H OH Undo Reset ―CH2OH- Remove Done ⚫SH CHO +arrow_forwardΔG°′ for the isomerization reaction glucose-1-phosphate (G1P) ⇌ glucose-6-phosphate (G6P) is −7.1 kJ · mol−1. Calculate the equilibrium ratio of [G1P] to [G6P] at 25°C.arrow_forwardThe ΔG°’ for the aldolase reaction of glycolysis in muscle is +22.8 kJ/mol. Why does the aldolase reaction proceed in the direction of glyceraldehyde-3-phosphate and dihydroxyacetone phosphate during glycolysis?arrow_forward
- The turnover number of the enzyme fumarase that catalyzes the reaction, Fumarate + H20 ===→ L-malate, is 2.5 x 103 S - l and Km = 4.0 X 10- 6 mol/L. Calculate the rate of conversion of fumarate to L-malate if the fumarase concentration is 1.0 x 1 0 - 6 mol/L and the fumarate concentration is 2.04 x 10- 4 mol/L.arrow_forwardThe high phosphoryl transfer potential of 1,3-bisphosphoglycerate is explained by the resonance stability of the product, 3-phosphoglycerate. The same explanation applies to the reaction that generates resonance stabilized pyruvate from phosphoenolpyruvate. Show the resonance structures for both products, 3-phosphoglycerate and pyruvate, and state why the reactant in both reactions is not resonance stabilized.arrow_forwardThe 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-alaninearrow_forward
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ISBN:9781305577206
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Publisher:Cengage Learning