Will someone please answer all the parts to question 5-5 and include all of the
ID: 84894 • Letter: W
Question
Will someone please answer all the parts to question 5-5 and include all of the work as well, please. Thank you!
the above reaction as carried out by a photosynthetic algal cell that is using CO2 and H2O to make C6H12O6? The Equilibrium Constant. The following reaction is one of the steps in the glycolytic pathway, which we will encounter again in Chapter 9. You should recognize it already, however, because we used it as an example earlier (reaction 5-6): glucose-6-phosphate fructose-6-phosphate (5-25) The equilibrium constant Keg for this reaction at 250C is 0.5 (a) Assume that you incubate a solution containing 0.15 M glucose-6-phosphate (G6P) overnight at 250C with the enzyme phosphoglucoisomerase that catalyzes reaction 5-25 How many millimoles of fructose-6-phosphate (F6P) will you recover from 10 ml of the incubation mixture the next morning, assuming you have an appropriate chromato graphic procedure to separate F6P from G6P? (b) What answer would you get for part a if you had started with a solution containing 0.15 M F6P instead? (c) What answer would you expect for part a if you had started with a solution containing 0.15 M G6P but forgot to add phosphoglucoisomerase to the incubation mixture? (d) Would you be able to answer the question in part a if you had used 15°C as your incubation temperature instead of 25C? Why or why not? 5-6 Calculating AGo' and AG. Like reaction 5-25, the conver ston of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2pG) is an important cellular reaction because it is one of the steps in the glycolytic pathway (see Chapter 9):Explanation / Answer
a) you have added 150 mM G6P. and Keq= 0.5.
so at equilibrium, both G6P and F6P will be half that is 75 mM.
b) we will get a mixture of G6P and F6P at equilibrium having 75 mM each.
c) enzyme is required for the conversion of G6P to F6P or vice versa. if we do not add enzyme then product will not be formed and reactant will be present at same concentration 150 mM.
d) if you change the optimal temperature of the enzyme then the reaction will go slow down but there is no change in equilibrium.
Related Questions
drjack9650@gmail.com
Navigate
Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.