The enzyme aldolase catalyzes the reaction shown in the glycolytic pathway:Fructose 1,6-bisphosphatedihydroxyacetone phosphate + glyceraldehyde 3-phosphateThe AG" for the reaction is +23.8 kJ mol¯¹ (+5.7 kcal mol−¹), whereas the AG in the cell is −1.3 kJ mol¯¹ (−0.3 kcal mol¯¹).Calculate the ratio of products to reactants under standard (equilibrium) conditions at 37°C.[products][reactants]7 x10-5[products][reactants]IncorrectAldolase=====Calculate the ratio of products to reactants under intracellular conditions at 37°C.4 ×10-5IncorrectComplete the statement using your results.under standard conditionsunder intracellular conditionsA reaction that is endergonic under standard conditions can be converted into an exergonic reaction by maintaining the ratioof products to reactants below the equilibrium value.

The ratio of concentration of products to reactants for any reaction in a given condition at…

Answered: The enzyme aldolase catalyzes the…

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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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.
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]
The reaction below occurs in nearly all human cells. It is catalyzed by the enzyme enolase. CO- CO- enolase -OPO3 OPO3 + H20 ČH,OH AGO'=+1.7 kJ/mol CH2 2PGA PEP Under cellular conditions, the AG is -3.3 kJ/mol. Which of the following could account for these changes in cellular AG compared to the standard biological free energy? The concentration of 2PGA is 7 times higher than PEP. The concentration of PEP is 7 times higher than 2PGA Enolase lowers the activation energy of the transition state. The release of water from 2PGA is a form of energy coupling.
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, fructose-1,6-biphosphate: 7mM %3D At what concentration of fructose-1,6-biphosphate would the reaction proceed backwards at 35°C?
Under standard conditions, is the oxidation of free FADH2 by ubiquinone sufficiently exergonic to drive the synthesis of ATP? (F = 96.5 kJ/V • mol) ubiquinone + 2H++ 2e¯ → ubiquinol E' = 0.045 V FAD + 2H++ 2e → FADH2 = E' -0.219 V ○ no, as oxidation of FADH2 by ubiquinone generates 33.6 kJ/mol ○ no, as oxidation of FADH2 by ubiquinone generates 50.9 kJ/mol ○ no, as oxidation of FADH2 by ubiquinone generates -25.5 kJ/mol ○ yes, as oxidation of FADH2 by ubiquinone generates -33.6 kJ/mol ○ yes, as oxidation of FADH2 by ubiquinone generates -50.9 kJ/mol
The conversion of dihyroxyacetone phosphate to glyceraldehyde 3-phosphate, catalyzed by triose phosphate isomerase, has an equilibrium constant of Keq’ = 0.0475. Calculate the standard free-energy change for this reaction at 25ºC and pH 7.0.
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
The isoelectric point (pI) of 6-phosphogluconate dehydrogenase is 6.0. Explain why the buffer used in DEAE cellulose chromatography must have a pH greater than 6 but less than 9 in order for the enzyme to bind to the DEAE resin.
Calculate AG for this reaction under the following conditions: 37°C, pH 7, [Pyruvate] = [CO₂] = 4.0 mM, [OAA] = 2.0 mM, [ATP] = 3.5 mM, [P;] = 5.0 mM, and [ADP] = 1.8 mM. Use 2 signficant figures. AG= i kJ.mol-1 Under these conditions, the reaction is (Tolerance is +/- 2%)
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
Crystals of phosphorylase a grown in the presence of glucose shatter when a substrate such as glucose 1- phosphate is added. Why?
When 10 micrograms of an enzyme with a molecular mass of 80,000 Daultons (grams/mol) is added to a solution containing its substrate at a concentration 100 times the Km, it catalyzes the conversion of 65 micromoles of substrate into product in 3 minutes. What is the enzyme's turnover number (in units of min-1)?

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