Q19: Phosphoglucoisomerase interconverts glucose 6-phosphate to, and from, glucose 1-phosphate.phosphoglucoisomeraseglucose 6-phosphateglucose 1-phosphateAfter mixing equal amounts of the two molecules, the solution achieved equilibrium at 25 °C. The concentration at equilibriumof glucose 1-phosphate is 0.01 M, and the concentration at equilibrium of glucose 6-phosphate is 0.19 M.Calculate the equilibrium constant, Keq, and the standard free energy change, AG, of the reaction mixture.Keq =AGⓇ =kJ. mol-¹

Answered: Phosphoglucoisomerase interconverts…

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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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
Given that the AG" values for the hydrolysis of glucose 1-phosphate and glucose 6-phosphate are approximately -21 kJ/mol and –14 kJ/mol, respectively, which statement is true regarding the isomerization shown? glucose 1-phosphate → glucose 6-phosphate O The reaction can likely proceed in either direction and will therefore depend on the concentrations of glucose 1-phosphate and glucose 6-phosphate. O Only the anabolic direction will occur because the free energy change is positive. O The reaction will proceed in both directions simultaneously. This reaction can only proceed in one direction and must be the rate limiting reaction for this point in metabolism.
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
Calculate the standard-state free energy change for the isomerization of glucose-1-phosphate to glucose-6-phosphate
80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pl. The solution is then titrated with 0.2M HCI to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCl needed to reach each relevant pKa value and equivalence point(s). Relevant pka values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
G6P(ag) F6P(aq) AG°=+1.7kJ/mol at 25 °C Consider the reaction: Estimate the fraction of F6P (Fructose 6 Phosphate) in equilibrium with G6P (Glucose 6 Phosphate) at 25 °C, where the fraction is defined as [F6P]/([F6P]+[G6P]). Show ALL your work.
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?
The effect of temperature on the hydrolysis of lactose by a ß-galactosidase is shown below in Table 1. The temperature coefficient, Q10 is the factor by which the rate increases by raising the temperature 10°C. The universal gas constant, R is 8.314 J/mol.K. (a) (b) Table 1: Data of Vmax over temperature T (°C) 20 30 35 40 45 Vmax (umoles/min.mg protein) 4.50 8.65 11.80 15.96 21.36 Plot the graph of In Vm vs 1/T using any spreadsheet software (include all appropriate labels and equation). Calculate the activation energy Ea and temperature coefficient Q10.
Consider the following reaction: Glucose 6-phosphate + Glucose 1-phosphate After reactant and product were mixed and allowed to reach equilibrium at 25C, the concentration of each compound was measured: (Glucose 1-phosphate] - 0.002 M [Glucose 6-phosphate 0.05 mM Calculate the Keg and the AG knot prime (e.g. standard free energy change). O Keg- 40: AG knot prime 9.14 kJ/mol O Ken- 19: AG knot prime -7.3 kJ/mol O Keg" 0.04: AG knot prime-7.98 kJ/mol Kea 4: AG knot prime -914 kJ/mol O Keg 40: AG knot prime - 9.14 k/mol
The isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde 3-phosphate (GAP) is catalyzed by triose phosphate isomerase. In the cell, the concentration ratio of DHAP/GAP = 5.5. Calculate [DHAP] (in M) when [GAP] = 0.00002
Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…
The following table shows the molecular masses (Mr) and isoelectric points (pI) of five proteins: Protein Mr pI Chicken egg white lysozyme 14,000 11.0 Carbonic anhydrase 30,000 5.4 Ovalbumin 45,000 4.5 Phosphorylase b 97,000 6.7 Lactate dehydrogenase 140,000 7.12 (a) A solution containing these five proteins was adjusted to pH 7.0 and then applied to a SIZE-EXCLUSION COLUMN. Assume that these five protein molecules are spherical in shape. Which protein is likely to be eluted LAST from the column? Explain briefly. (b) In another experiment, this protein mixture was first adjusted to pH 6.7 before applying to a CATION-EXCHANGE COLUMN. (i)What is the net charge on phosphorylase b? (ii) Which of these five proteins will bind to the CATION-EXCHANGER? Explain briefly.v

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