Triose phosphate isomeraseIn a key reaction of glycolysis, dihydroxyacetone phosphate (DHAP) is isomerized intoglyceraldehyde 3-phosphate (G3P) by the action of the enzyme triose phosphate isomerase:CH₂OHC=OCH₂OPO3²-DHAPCHOHC-OHCH₂OPO3²-G3PAG°¹ +7.5 kJ/molBecause AG is positive, the equilibrium lies to the left.(a) Calculate the equilibrium constant for this reaction, assuming a temperature of 37 °C.(b) In the cell, depletion of G3P makes the reaction proceed. What is the value of AG if theconcentration of G3P is kept at 1/100 of the value of the concentration of DHAP?CZOOM+

Given Values: ∆G°=7.5 kJ/mol or 7500 J/molT = 37°C or 310 KR = 8.314

Answered: Triose phosphate isomerase In a key…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter20: Electron Transport And Oxidative Phosphorylation

Section: Chapter Questions

Problem 2P

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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?
Consider 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·mol
Acetyl CoA + 2H* + 2e = pyruvate + COASH E = -0.48 V Ubiquinone + 2H* + 2e = Ubiquinol E" = +0.04 V Consider the redox rxn wherein a pair of e passes from pyruvate to ubiquinone. Calculate the change in standard Gibbs free energy (kJ/mol). Report answer to two decimal places.
Standard redox potentials Eo' for some common compounds in biochemistry: Eo' (Volt) + 0,81 +0,42 + 0,25 12 O₂ + 2 H+ + 2 e NO3 + 2 H+ + 2 e 2 cyt c (ox) + 2 e 2 cyt b (ox) + 2 e Pyruvate + 2 H+ + 2 e* NAD + 2 H+ + 2 e Acétoacétate + 2 H+ + 2 e (2) acétoacétate + NADH + H+ H₂O NO₂ + H₂O 2 cyt c (red) 2 cyt b (red) Lactate (3) 2 cyt c (ox) + 2 cyt b (red) NADH + H+ B-hydroxybutyrate + 0,08 - 0,19 With the help of the above table, determine the spontaneous direction of the following reactions in the standard conditions. Justify your answers by calculating the Gibbs (free) energy of reaction in each case. (1) pyruvate + ß-hydroxybutyrate -0,32 - 0,35 lactate + acétoacétate B-hydroxybutyrate + NAD+ 2 cyt c (red) + 2 cyt b (ox)
Please provide an explanation for how to work through this practice problem: Using table 12.1, calculate the free energy change for the synthesis of ATP from cAMP and inorganic phosphate. (Note: cAMP is hydolyzed to AMP, and the free engery of hydrolysis for ATP and ADP is approximately equal.) Table 12.1: (Compound: Change in Free Energy in kJ/mol) cAMP: -50.4 Creatine phosphate: -43.3 ATP: -30.5 Glucose 6-phosphate: -13.9 AMP: -9.2
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;) -30.5
The 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.
Arrange the balanced biochemical equations for all the reactions in the catabolism of glucose to two molecules of glyceraldehyde 3-phosphate (the preparatory phase of glycolysis). First step Last step Answer Bank Fructose 1,6-bisphosphate - dihydroxyacetone phosphate + glyceraldehyde 3-phosphate Fructose 6-phosphate + ATP →→→→ fructose 1,6-bisphosphate + ADP Glucose + ATP → glucose 6-phosphate + ADP Dihydroxyacetone phosphate glyceraldehyde 3-phosphate Glucose 6-phosphate →→→→ fructose 6-phosphate
Calculate the standard free energy for creatine-phosphate hydrolysis in a cell where [creatine-P]=3 mM, [creatine]=2 mM, and [Pi]= 12.1 mM. Is the reaction exergonic or endogonic?
Determine 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!
ΔG°′ 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.
A new drug, Proinebrium, that reduces Kcat (Ki = 2.0 uM) has been developed to treat ethylene glycol poisoning. (1) What concentration of Proinebrium is required to achieve 50% inhibition of ethylene glycol metabolism by alcohol dehydrogenase when the concentraion of ethlyene glycol in the blood is 50 uM?

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