In glycolysis, fructose 1,6-bisphosphate is converted to two products with a standard free-energy change (AG) of 23.8 kJ/mol. Under what cellular conditions will the free-energychange be negative, enabling the reaction to proceed spontaneously to form products?O In a cell where the concentrations of products and reactants yield a low value of the mass-action ratioQ○ The reaction will not go to the right spontaneously under any conditions because the AG is positive○ The reaction will proceed spontaneously to the right if there is a high concentration of productsrelative to the concentration of fructose 1,6-bisphosphate○ The reaction will proceed spontaneously to the right if there is a high concentration of enzyme tocatalyze the reactionO None of these conditions is sufficient

under what cellular conditions the free-energy change (ΔG) will be negative, we need to consider the…

Answered: In glycolysis, fructose…

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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Table 1 shows the kinetic data that have been obtained for glucoamylase from Aspergillus niger at different temperatures in the production of glucose from maltodextrin. The rates of reaction measured are using an enzymes concentration of 0.003 μmolml-1. Outline and describe the reaction scheme of the production of glucose from maltodextrin by using glucoamylase.
Given the following reaction and equation for the initial velocity of the reaction: k₁ k3 E+S ES E + P V=Keat [ES] = k3 [ES] k₂ where keat is the rate constant for the reaction which forms the product from the ES complex. Explain in words why the velocity is directly proportional to theamount of enzyme added in the presence of saturating substrate levels.
The first reaction in glycolysis is the phosphorylation of glucose to form glucose 6-phosphate: P₁+ glucose glucose 6-phosphate + H₂O This is a thermodynamically unfavorable reaction, with AG° = +13.8 kJ/mol. a) In a liver cell at 37°C the concentrations of both phosphate and glucose are normally maintained at about 5 mM each. What is the equilibrium concentration of glucose 6- phosphate, according to the above reaction? b) This very low concentration of glucose 6-phosphate is unfavorable for glycolysis. In fact, the reaction is coupled to the hydrolysis of ATP: ATP + H₂O2 ADP + P₁ +H* AG°¹ = -32.2 kJ/mol Write the expression for the overall reaction and calculate AG°¹. c) In addition to the glucose and phosphate concentrations listed in part (a) above, assume that the liver cell concentrations of ATP and ADP are 3 mM and 1 mM, respectively. Calculate the theoretical equilibrium concentration of glucose 6-phosphate at pH = 7.4 and 37 °C. C ZOOM +
An enzyme catalyzes a reaction with a K of 7.50 mM and a Vmax of 4.15 mMs. Calculate the reaction velocity, o, for each substrate concentration. [S] = 1.75 mM MM-s-1 [S] = 7.50 mM [S] = 11.0 mM DO mM-s mM-s
The reaction catalyzed by phosphorylase is readily reversible in vitro. At pH 6.8, the equilibrium ratio of orthophosphate to glucose 1-phosphate is 3.6. The value of ΔG°’ for this reaction is small because a glycosidic bond is replaced by a phosphoryl ester bond that has a nearly equal transfer potential. However, phosphorolysis proceeds far in the direction of glycogen breakdown in vivo. Suggest one means by which the reaction can be made irreversible in vivo.
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]
1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?
Acetyl CoA + 2H* + 2e = pyruvate + COASH E = -0.48 V Ubiquinone + 2H* + 2e = Ubiquinol E" = +0.04 V Consider the redox rxn wherein a pair of e passes from pyruvate to ubiquinone. Calculate the change in standard Gibbs free energy (kJ/mol). Report answer to two decimal places.
Many metabolites are maintained at steady‑state concentrations that are far from equilibrium. A comparison of ?′eq and ? , the mass‑action ratio, can determine whether a metabolic reaction is far from equilibrium. The equation for this equilibrium is, fructose 6-phosphate+ATP↽−−⇀fructose 1,6-bisphosphate+ADPCalculate ?′eq for this reaction at ?=25.0 ∘C . Δ?∘′=−14.2 kJ/mol ?′eq=
Can you graph the data
You begin to study enzyme Z, which catalyzes a simple reversible reaction that interconverts compound S and compound P. You observe that the ∆G´° for the S to P conversion to be –6 kJ/mol, and that compound S has ∆G´° for binding to enzyme Z of –15 kJ/mol, while compound P has a ∆G´° for binding to enzyme Z of –13 kJ/mol. Please explain the effect of enzyme Z on conversion of S to P. (Your answer should include a graph qualitatively showing energy versus reaction progress; however, you still need to explain youranswer in words!) not sure how to make the correct graph.
The following nutrient molecule is digested and transported to a cell where it undergoes further catabolism: но c-(CH;)14-CH3 di In the table below, list the important products of the complete B oxidation of this molecule. • In the first column of the table, write the chemical formula, name, or standard biochemical symbol for a product molecule. In the second column, write the total number of these molecules produced. • Only list the Important products, including (1) molecules with any of the carbon atoms that were in the original molecule, (2) energy storage molecules (like ATP), and (3) newly oxidized or reduced coenzymes. List each product molecule on a separate row. You can add more rows if you need them. • Be sure you write the number of product molecules formed by the complete B oxidation of the molecule above. • Do not include the products of any catabolic activity that happens before or after B oxidation, including any necessary activation. If the molecule contains small parts…

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