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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a particular enzyme catalyzes a single reactant S to a single product P, following michaelis-menten kinetics rp=(VmaxCs) / (Km + Cs) 1. A reaction with this enzyme is carried out at very low substrate concentrations. Draw and label a curve on the plot that describes the reaction kinetics under those conditions.
Consider an enzyme that follows standard Michaelis-Menten kinetics and has the following kinetic constants: %3| k2 = 1.5 x 10? s1 Еo 3D 1 х 104 М = 1 x 104 M a. What is the value of the maximum rate VM? b. Prepare a hand-drawn quantitative plot on graph paper (not a simple sketch nor an EXCEL-generated graph) of the enzymatic reaction rate versus substrate concentration (like Fig 3-3) using the kinetic parameters given above. Be sure to label the axes and include numeric values on the axes. C. Based upon your hand drawn saturation plot, at what substrate concentration is the enzymatic reaction rate 75% of Vm?
24. Hexokinase catalyzes the phosphorylation of glucose from ATP, yielding glucose-6-P and ADP. The standard-state free energy change for hydrolysis of glucose-6-P is -13.9 kJ/mol. Calculate the standard-state free energy change and equilibrium constant for the hexokinase reaction. AG" for ATP hydrolysis -31.5 kJ/mol
The O2-consumption curve of a dilute, well-buff ered suspension of mito chondria containing an excess of ADP and Pi takes the following form: Sketch the curves obtained when (a) amytal is added at time t = 1 and (b) amytal is added at t = 1 and succinate is added at t = 2.
The reaction in which glucose 6-phosphate (G6P) is converted to fructose 6-phosphate (F6P) is an example of an isomerization reaction. Notice that both molecules have the molecular formula C6H13O9P. The isomerization is catalyzed by glucose 6-phosphate isomerase. This is a reversible reaction in cells, with a moderately negative ΔG, but a very high activation energy. If you have a flask that contains a solution containing cellular concentrations of G6P and F6P, but no enzyme, how will the concentration of each molecule change over time?
You are working on an enzyme that obeys standard Michaelis-Menten kinetics. Based on the following reaction expression, what is the Km value for this enzyme? E+SESE + P . . . k₁ = 880.8 M-¹5-1 k.₁ = 42.18 S-1 k₂ = 56.29 S-1
what is the Vmax and Km of the enzyme in the reaction asap please.
NOTE: the enzyme-inhibitor complex requires 450 joule/mol to dissociateJOULE/MOL
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. Table 1: Glucoamylase Activity at different temperatures Maltodextrin Concentration (μmol/L) 0.5 1 1.5 2.2 5.5 11 Initial Reaction Velocity (μmol/L.s) T = 40°C 2.1 3.5 4.9 5.6 589 8.3 9.3 T = 60°C 5.2 9.7 13 16 23 31
Consider an enzyme (P) that gets activated by forming a dimer (P2): 2P = P2 At 25 °C, we have AH- 19 kJ/mol and AS-65 kJ/mol, for this dimerization reaction. Identify the correct statement. O The enzyme is activated when kept at temp = +37 °C. O The enzyme is activated at all temperatures. O The enzyme is activated when kept in the fridge with temp = 4 "C. O The enzyme can never be activated, no matter what the temperature is. O None of the above statements is true.

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