fructose-6-phosphate + ATP <-> fructose-1,6-biphosphate + ADPAG° = 30.5 and 16.3 respectivelyStandard Free Energy change: -14.2 kj/molATP: 3mM, ADP: 0.4mM, fructose-1,6-biphosphate:7mM%3DAt what concentration of fructose-1,6-biphosphatewould the reaction proceed backwards at 35°C?

The Gibbs free energy (G): It is the thermodynamic function that best captures the energetics of…

Answered: fructose-6-phosphate + ATP <->…

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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A key step in the biosynthesis of triglycerides (fats) is the conversion of glycerol to glycerol-1-phosphate by ATP: At a steady state in the living cell, (ATP) = 10-3M and (ADP) = 10-4 M. The maximum (equilibrium) value of the ratio (glycerol-1-P)/(glycerol) is observed to be 770 at 25 °C and pH=7. Calculate K and DrG° for the reaction. Using the value of DrG° for the reaction ADP + Pi àATP + H2O, together with the answer to part (a), calculate DrG° and K for the reaction: glycerol + phosphateà glycerol-1-phosphate+ H2O .
Consider the graphic representation shown below for the free energy change for the overall reaction of Fructose-6-phosphate and ATP to form the products Fructose-1,6-biphosphate and ADP in the presence (blue line) or absence (red line) of enzyme. Match each of the arrows (labeled A, B, C, or D) indicated in the graph with an apropriate description by dragging the letters into their corresponding box. C D reactants Fructose-6-phosphate + ATP A products Fructose-1,6-biphosphate + ADP Progress of the Reaction Reset Help D BAc В C Energy of activation for the forward reaction in the absence of enzyme Energy of activation for the forward reaction Energy of activation for the reverse reaction in absence AG for the reaction the presence of enzyme of enzyme Energy
Free energy changes under intracellular conditions differ markedly from those determined under standard conditions. AG" =-30.5 kJ/mol for ATP hydrolysis to ADP and P,. Calculate AG for ATP hydrolysis in a cell at 37 °C that contains [ATP] =3 mM, [ADP] =1mM, and [P] =1 mM.
As a result of an experiment following measurements were obtained from a cell: ATP concentration of 0.5 mM, ADP concentration of 0.1 mM, inorganic phosphate (Pi) concentration of 2 mM. Under these conditions calculate the actual free energy (AG) of the reaction of hydrolysis of ATP to ADP and Pi. (The standard energy (AG") of ATP = -31 kl/mol; RT = 2.58 kJ/mol) Select one: a. -28 kJ/mol b. -33 kJ/mol C. -42 kJ/mol d. -19 kJ/mol
Calculate the ATP yield for the full catabolism of a phospholipid containing ethanolamine, C18:3 Δ9, 12, 15 and oleic acid. Include any ATP “expenses” or “income”. This will be a complex problem—neatly show your work and justify your choices.
Intramitochondrial ATP concentrations are about 5 mM, and phos- phate concentration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentra- tion of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]
1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?
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
Following is a Dixon plot for PNPP inhibition by inorganic phosphates. What answer choice shows the correct combination of the mode of inhibition and Ki of the EI complex? - Mixed inhibition, Ki= -21.2 uM - Mixed inhibition, Ki= 1/16.5 uM - Competitive inhibition, Ki= 16.5 uM - Competitive inhibition , Ki= -1/16.5 uM - None of the above
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.
If 287.9 umol of enzyme X has a Vmax = 47.8 mmol/sec, what is the value of kcat %3D sec-1? Please report answer with 1 decimal place. Please do not report units. Your Answer: Answer units MacBook Air 888 F5 F4 F3 F2 %23 %24 %24
Assume that in a certain cell, the ratio of products/reactants or Keg = 809.5 (Keq is dimensionless) for the reaction Glucose + 2ATP > Glucose-1,6-diP + 2ADP, at a particular instant, the concentrations of each compound were Glucose =2.4M, ATP =11.1M, ADP -12.8M and G-6-P -28.4M. Calculate the difference (dimensionless) between Keq and the ratio of products/ractants at this instance, in this cell, to five decimal places

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fructose-6-phosphate + ATP <-> fructose-1,6- biphosphate + ADP AG = 30.5 and 16.3 respectively Standard Free Energy change: -14.2 kj/mol ATP: 3mM, ADP: 0.4mM, 7mM fructose-1,6-biphosphate: At what concentration of fructose-1,6-biphosphate would the reaction proceed backwards at 35°C?