1. Hydrolysis of 1 M glucose 6-phosphate catalyzed by glucose 6-phosphatase is 99% complete atequilibrium (i.e., 1% of the substrate remains). Which of the following statements is most nearlycorrect? (R= 8.315 J/mol-K; T = 298 K)A AG" is-11 kl/mol.B) AG" is +5 kJ/mol.C) AG" is 0 kJ/mol.DAG" is +11 kJ/mol.E) AG" cannot be determined from the information given.Explain your choice in one line:-2.16x298 (2)- 11386.15-> 11.4 КТ5The high state conculto alle My negative and st" positive (either for D) thenonditions, one

Standards free energy change calculated at biochemical standards is called biochemical standard free…

Answered: 1. Hydrolysis of 1 M glucose…

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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The conversion of glucose-1-phosphate to glucose-6-phosphate by the enzyme phosphoglucomutase has a △G°' of -7.6 kJ/mol. Calculate the equilibrium constant for this reaction at 298 K and a pH of 7. (R = 8.315 J/K-mol) A. 0.003 B. 0.047 C. 1.00 D. 21
Assume that you have a solution of 0.1 M glucose 6-phosphate. To this solution you add the enzyme phosphoglucomutase, which catalyzes the reaction: glucose-6-P ⇔ glucose-1-P ∆G°′ = +1.7 kJ/mol (a) Does this reaction proceed at all as written at 25 °C, and if so, what are the final concentrations of glucose 6-P and glucose 1-P? (b) What effect would omitting the enzyme have on the reaction. Be specific. (c) Under what cellular conditions, if any, would this reaction continuously produce glucose 1-P at a high rate?
A) Is this reaction ( in picture provided) in equilibrium? B) If it is not then ,what is ∆G' at 25°C if the concentration of Glucose-1-phosphate is 15.04µM and the concentration of Glucose-6-phosphate is 1.62 mM? Answer in Joules. Round to the correct number of significant figures. (There are 103 µM in 1mM.) Thank you so Much!!!
A bacterial enzyme catalyzes the hydrolysis of maltose as shown in the reaction given below: Maltose + H2O -> 2 glucose If the reaction has a Km of 0.135 mM and a V max of 65 umol/min. What is the reaction velocity when the concentration of maltose is 1.0 mM? (Please take note of the units)
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 Calculate Keq and ΔG′° for this reaction.
In the reaction ATP + glucose → ADP + glucose-6-phosphate, ΔG° is -16.7 kJ/mol. Assume that both ATP and ADP have a concentration of 1 M and T = 25°C. What ratio of glucose-6- phosphate to glucose would allow the reverse reaction to occur?
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.
1. Assuming that everything that’s needed to make tripalmitin comes from glucose, how many glucose would be used by adipose tissue in the synthesis of 1 mol tripalmitin? 2. How many ATP would be used (net of produced and used)? 3. If an animal absorbs 35 g glucose (MW = 180 g/mol) from drinking a can of pop, how many grams of tripalmitin (MW = 807 g/mol) can be produced from it in adipose tissue? Please provide only typed answer solution no handwritten solution needed allowed
The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"
One of the examples that we have used to illustrate the concept of equilibrium is the isomerization of glucose-6-phosphate (G6P) to fructose-6-phosphate (F6P), which is the second step in g ycolysis. Draw a graph to show how the reaction Gibbs energy varies with the fraction fof F6P in solution.Label the regions of the graph that correspond to the formation of F6P and G6P being spontaneous, respectively.
The hydrolysis of ATP to ADP has a △G°' of -30 kJ/mol. If in an E. coli cell the concentrations of ATP, ADP and inorganic phosphate are 7.90 mM, 1.04 mM and 7.9 mM, respectively, which statement is true about the hydrolysis of ATP in the cell? (Assume a temperature of 298 K. R = 8.315 J/K-mol) A. The formation of ATP from ADP is occurring more rapidly than the hydrolysis. B. The hydrolysis is being allosterically controlled. C. Hydrolysis can proceed spontaneously. D. The hydrolysis is at equilibrium. QUESTION 10 The conversion of glucose-1-phosphate to glucose-6-phosphate by the enzyme phosphoglucomutase has a △G°' of -7.6 kJ/mol. Calculate the equilibrium constant for this reaction at 298 K and a pH of 7. (R = 8.315 J/K-mol) A. 0.003 B. 0.047 C. 1.00 D. 21 help with these questions please
Consider the following chemical equation whose delta(G) = 9kcal/mol: AC + BD ---> AB + CD what are the reactants and what are the products is this reaction spontaneous? How do you know? Is energy released or consumed by this reaction? If an enzyme, which catalyzes this reaction is added, what will happen to delta (G) If this reaction is coupled to another reaction, whose delta(G) is -12 kcal/mol, what will be the net delta(G) value? will the overall reaction be spontaneous

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