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What is △Go of Reaction #3?
What is the Keq of Reaction #3?
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Is Reaction #3 favorable under mammalian cellular conditions when the concentration of dGTP is 0.2 M, dCMP is 20 mM, dGMP-dCMP is 7 mM, and PPi is 10 mM? Use △G to support your answer. Show your work and clearly label your final answer.
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- Neutral sphingomyelinase 2 converts sphingomyelin into ceramide and phosphorcholine. What kind of enzyme is it? Assume Vmax is 35 µM min-1. When you provide 3.0 x 10-5 M of sphingomyelin, you observe an initial velocity of 6.0 µM min-1. Calculate the KM.a) (1) Calculate the physiological AG (not AG.) for the reaction: Phosphocreatine + ADP - creatine + ATP Given; Phosphocreatine + H;0 - creatine + Pi ADP + Pi → ATP + H;0 AG.' -43 kJ/mol AG.- +30.5 kJ/mol at 25°C as it occurs in the cytosol of neurons, in which phosphocreatine is present at 4.7 mM, creatine at 1.0 mM, ADP at 0.20 mM, and ATP at 2.6 mM. (R = 8.315 JK-' mol-) (ii) Caleulate the free energy change at standard conditions for the following reaction: Acetaldehyde + NADH + H* + Ethanol + NAD* The half- reactions are: Acetaldehyde + 2H + 2e + Ethanol E°- - 0.20V NAD-+ 2H- + 2e ++ NADH + H- E=-0.32V (F= 96.485 kJ/V/mol)Using the Nernst equation, calculate the equilibrium potential for Ca2 and for C1 from the following sets of data: a. Given [ Ca2+ ]0=1mM,[ Ca2+ ]i=100nM, find Eca2+ b. Given [ Cl- ]0=110mM,[ Cl- ]i=100mM, find Ecl
- Calculate ΔG°′ for the reaction A + B ⇌ C + D at 25°C when the equilibrium concentrations are [A] = 10 μM, [B] = 15 μM, [C] = 3 μM, and [D] = 5 μM. Is the reaction exergonic or endergonic under standard conditions?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·molMany enzymes obey simple Michaelis–Mentenkinetics, which are summarized by the equationrate = Vmax [S]/([S] + Km)where Vmax = maximum velocity, [S] = concentration ofsubstrate, and Km = the Michaelis constant.It is instructive to plug a few values of [S] into theequation to see how rate is affected. What are the rates for[S] equal to zero, equal to Km, and equal to infinite concen-tration?
- Calculate the rate enhancement for the enzyme pair: Enzyme 1: Kcat (sec-1)= 5.5 KM (µ M) = 1245 Kcat / KM = 0.00442 (µ M-1 sec-1) Enzyme 2: Kcat (sec-1)= 3.2 KM (µ M) = 1785 Kcat / KM = 0.00179 (µ M-1 sec-1)a) The equilibrium reaction for the aqueous dissociation of acetic acid is shown below. CH3COOH(aq) = CH3COO-(aq) + H+ (aq) Given the data in the table below and your knowledge of the "chemical standard state" (X) and the “biochemical standard state” (Xº'), answer parts a) to e). c) For the dissociation of acetic acid at 298.15 K, calculate AG and the corresponding pK₁. b) Even though by definition, AfG©(H+ (aq)) = 0 and_AƒGº¹(H+(aq)) = 0, these are different physical quantities. What precisely does each represent? Calculate at 298.15 K, AG' for CH3COOH(aq) and CH3COO¯(aq). Gibbs free energy of formation, in units of kJ mol-¹, at T = 298.15 K AfGe A¢G° -396.5 -369.3 0 CH3COOH(aq) CH3COO- (aq) H+ (aq) d) For the dissociation of acetic acid at 298.15 K, calculate ArGº¹. LOXF 0 Finally, using the formula to convert between standard states, show that that your calculated values of AG and A.Gº are in agreement. jonly thisIntracellular concentrations in resting muscle are as follows: fructose- 6-phosphate, 1.0 mM; fructose-1,6-bisphosphate, 10 mM; AMP, 0.1 mM; ADP, 0.5 mM; ATP, 5 mM; and P, 10 mM. Is the phosphofructokinase reac- tion in muscle more or less exergonic than under standard conditions? By how much?
- In another key reaction in glycolysis, dihydroxyacetone phosphate (DHAP) is isomerized into glyceraldehyde-3-phosphate (GAP): CH,OH | C=0 НС — ОН AG" = +7.5 kJ/mol CH,OPO,?- CH,OPO,- DHAP GAP Because AG° is positive, the equilibrium lies to the left. (a) Calculate the equilibrium constant, and the equilibrium fraction of GAP from the above, at 37 °C. (b) In the cell, depletion of GAP makes the reaction proceed. What will AG be if the concentration of GAP is always kept at 1/100 of the concentration of DHAP?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)Intracellular concentrations in resting muscle are as follows: fructose6-phosphate, 1.0 mM; fructose-1,6-bisphosphate, 10 mM; AMP, 0.1 mM;ADP, 0.5 mM; ATP, 5 mM; and Pi, 10 mM. Is the phosphofructokinasereaction in muscle more or less exergonic than under standard conditions?By how much?