The equilibrium constant for the reaction below is 0.02 mol dm-3 at 298.000 K.Fructose 1,6-diphosphate _ glyceraldehyde 3-phosphate + dihydroxyacetone phosphateCalculate ΔG°.Provide answer to two decimal places and as J mol-1.

The equilibrium constant for the reaction below is 0.02 mol dm-3 at 298.000 K.Fructose 1,6-diphosphate _ glyceraldehyde 3-phosphate + dihydroxyacetone phosphateCalculate ΔG°.Provide answer to two decimal places and as J mol-1.

Chemistry: Principles and Reactions

8th Edition

ISBN:9781305079373

Author:William L. Masterton, Cecile N. Hurley

Publisher:William L. Masterton, Cecile N. Hurley

Chapter23: Organic Polymers, Natural And Synthetic

Section: Chapter Questions

Problem 46QAP: Glycolysis is the process by which glucose is metabolized to lactic acid according to the equation...

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Q2 CH,OH CH,OPO,2- H H OH H OH 0-PO,2- но но OH H. OH OH Glucose-1-phosphate Glucose-6-phosphate Calculate the standard free-energy change (AG°) fo the reaction catalyzed by the enzyme phosphoglucomutase. When at standard temperature (25 °C) and pressure, the equilibrium of each molecule is 1 mM glucose 1-phosphate and 19 mM glucose 6-phosphate. HINT: at 25 °C, RT = 2.479 kJ/mol
Calculate the equilibrium constant at 37oC for the reactionGlucose + 6O2 + 36ADP + 36Phospate → 6CO2+ 42H2O +36ATP ... ... ...Entropy change of Go= − 423 kcal/mole of Glucose
3. Hexokinase catalyzes the first reaction in glycolysis and phosphorylates D-glucose to D-glucose 6-phosphate using ATP as the source of the phosphate. Under conditions of pH 7, 25°C and a Hexokinase concentration of 3.0 nmol/mL, the KM for Hexokinase for the substrate glucose was determined to be 3.0 x 10 M. a. When the glucose concentration was set to 160 μM, the initial rate of the reaction was found to be 65.0 μmol/(mL s). What is Vmax for Hexokinase under these conditions? b. What is the turnover number for Hexokinase under these conditions? c. What is the catalytic efficiency for Hexokinase under these conditions?
One of the important reactions in the biochemical pathway glycolysis is the reaction of glucose-6-phosphate (G6P) to form fructose-6-phosphate (F6P): G6P F6P AG-1.7 kJ Phosphoglucose Isomerase 6 CH2OPO, 2- H. CH2OPO3 ICH,OH H. H. HO. H. 1. H. HO. HO. H. 14 B OH H. H. HO. gluco se-6-phosphate fructo se-6-phosphate Standard thermodynamic conditions imply the concentrations of G6P and F6P to be 1 M, however, in a typical cell, they are not even close to these values. Calc kJ when the concentrations of G6P and F6P are 60.0 ×10M and 14.0 x10 M respectively, assume the temperature is 37 °C. (R = 8.314 J/K-mol) O a. -0.1 kJ Ob.-1.1 kJ Oc.-2.1 kJ O d.-3.1 kJ O e.-4.1 kJ
Chemistry 3.Calculate the amount of free energy required (or released) to allow electron transport in the ETC to be spontaneous from NADH to ubiquinone under standard conditions based on two electrons moving through the system. This occurs at 25°C. ½ O2 + 2e + 2H+ ® H2O E°´ = 0.815 V NAD+ + 2e +H+ ® NADH E°´ = -0.315 V NADP+ + H+ + 2e ® NADPH E°´ = -0.320 V FAD + 2e +2H+ ® FADH2 E°´ = -0.219 V Ubiquinone + 2H + 2e ® Ubiquinol E°´ = 0.045 V
1. Calculation of AG from an Equilibrium Constant Calculate the standard free-energy change for each of the following metabolically important enzyme-catalyzed reactions, using the equilibrium constants given for the reactions at 25 °C and pH 7.0, R = 8.315 J/molK Aspartate aminotranterase (a)Glutamate + oxaloacetate 2 aspartate + a-ketoglutarate Keg-6.8 Triosephosphate isomerase (b)Dihydroxvacetonephosphate glyceraldehyde3phosphate Keg-0.0475 phosphofructokinase e fructose1,6-bisphosphate+ADP Keg=254 (c)Fructose6-phosphate + ATP
The hydrolysis of pyrophosphate to orthophosphate drives biosynthetic reactions such as DNA synthesis. In Escherichia coli, a pyrophosphatase catalyzes this hydrolytic reaction. The pyrophosphatase has a mass of 120 kDa and consists of six identical subunits. A unit of activity for this enzyme, U, is the amount of enzyme that hydrolyzes 10 umol of pyrophosphate in 15 minutes. The purified enzyme has a Vnax of 2800 U per milligram of enzyme. When (S] >> KM, how many micromoles of substrate can 1 mg of enzyme hydrolyze per second? Vnax = umol -s. mg- If cach enzyme subunit has one active site, how many micromoles of active sites, or (E]r, are there in 1 mg of enzyme? (Er = umol - mg-
A protein has a stability ranging from 6 to 15 kcal/mole at 37 OC. Stability is a measure of the equilibrium between the folded and unfolded protein given by the relationship; folded(F) = unfolded (U), k=[U]/[F] For a protein with a stability of 10 kcal/mole, calculate the fraction of unfolded protein that would exist at equilibrium at 37 OC. Use the following equation: ∆GO=RTlnk=-2.3RTlog k, where R=1.98 x 10-3kcal/mole and T is temperature in Kelvin (K) and k is the equilibrium constant.
This is a thermodynamically unfavorable process, with ΔG°' = +13.7 kJ/mol. In a liver cell at 37°C the concentrations of both phosphate and glucose are normally maintained at about 6.2 mM each, while the glucose-6-phosphate is around 2.1 mM . Calcaulate the Gibb's Free Energy (ΔG) of this reaction occuring in the liver
One pathway for the metabolism of D-glucose 6-phosphate is its enzyme-catalyzed conversion to D-fructose 6-phosphate. Show that this transformation can be accom- plished as two enzyme-catalyzed keto-enol tautomerisms. СНО CH,OH C=0 enzyme catalysis Но Но H OH H H. O- H- -HO- ČH,OPO, ČH,OPO, D-Glucose 6-phosphate D-Fructose 6-phosphate
H H-C-OH HO-C-H H²-OH H-C-OH 6 CH₂-OH D-(+)-glucose rotate H 6 5 C-CH₂-OH HI OH OH I OH C H 21 OH H H CH₂-OH -OH OH H H OH = H OH CH₂-OH 5 H OH H H ß (a) OH (H) H (OH) OH anomeric carbon D-glucopyranose 1. Redraw wrapping from C1-C6 clockwise. Keep all things on the right of the Fisher projection pointing down, all things on the left pointing up.
2. Experimental Determination of Keq' and AG If a 0.1 M solution of glucose 1-phosphate at 25 °C is incubated with a catalytic amount of phosphoglucomutase, the glucose 1-phosphate is transformed to glucose 6-phosphate. At equilibrium, the concentrations of the reaction components are Glucose1-phosphate glucose6-phosphate 9.6 x 10-2 M 4.5 x 10-3 M Calculate Keg' and AG for this reaction.