2.13Calculate the reaction enthalpy, entropy, and free energy, AH°,, ASº,, and AG°,, for theamidation of glutamate to glutamine (1) at standard temperature, (2) at 37°C, and (3) at 75°C (a)taking into account the temperature dependence of AH and AS, and (b) assuming that AH and AS aretemperature-independent. What can you conclude about the importance of Cp? What does the resultmean for organisms that live at moderate temperature (37°C; mesophilic organisms) andthermophilic organisms that live at 75°C?Glutamine: AH°; = -826 kJ mol², Cp,m = 184 J mol1 K1, Sm = 195 J mol1 K1f%3=Glutamate: AH°; = -1010 kJ mol1, Cp,m = 175 J mol1 K1, Sm = 188 J mol1 K1H2O: AH°¡ = -290 kJ mol1, Cp,m = 75 J mol1 K1, Sm = 70 J mol1 K1NH,*: AH°; = -133 kJ mol1, Cp,m = 80 J mol1 K1, Sm = 113 J mol1 K1%3D

Reaction thermodynamics is the energy things that occur during a chemical reaction together with a…

Answered: 2.13 Calculate the reaction enthalpy,…

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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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 following initial-rate data were obtained on the rate of binding of glucose w ith the enzyme hexokinase (obtained from yeast) present at a concentration of 1.34 mmol dm-3. What is (a) the order of reaction with respect to glucose. (b) the rate constant?[C6H12O6]/(mmol dm-3) 1.00 1.54 3.12 4.02vo/(mol dm-3 s-1) 5.0 7.6 15.5 20.0
5) In an experiment to investigate the inhibition of the enzyme-glucosidase the following data for the rates of reaction with glucopyranoside for various substrate concentrations was obtained. By constructing a Leaver-Burk plot, determine the value of the Michaelis constant. [S]/ (10-6 mol dm-3) v/ (10-3 mol dm-3 s-1) 1.00 2.00 3.00 4.00 16.7 33.3 41.1 49.8
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
The following kinetic data were obtained for an enzyme in the absence of an inhibitor (1) and in the presence of two different inhibitors (2) and (3) at 5mM concentration. [S], mM (mmol/mL/sec) (mmol/mL/sec) (mmol/mL/sec) (1) (2) (3) 1 12 4.3 5.5 2 20 8 9 3 29 14 13 8 35 21 16 12 40 26 18 Determine the Vmax and KM of the enzyme Determine the type of inhibition.
23. The drug UTSAone was investigated as a possible inhibitor of a dehydrogenase enzyme that acts on pregnenolone as a substrate in steroid synthesis. The activity of the dehydrogenase was measured in the presence and in the absence of 10 µM UTSAone. Use the data in the table to construct a Lineweaver-Burk plot. [Pregnenolone, µM] Vo without I (pmol/min) Vo with I (pmol/min) 1.0 0.00106 0.00079 5.0 0.00327 0.00242 10.0 0.00439 0.00326 20.0 0.00529 0.00395 Which of the following statements are TRUE? A. The Km (uM) in the absence of UTSAone is 2.4. The Km (uM) in the absence of UTSAone is 5.4 В. The Km (uM) in the presence of UTSAone is 2.4. D. The Km (µM) in the presence of UTSAone is 5.3. The Vmax (pmol/min) in the absence of UTSAone is 6.8 x 103. F. The Vmax (pmol/min) in the presence of UTSAone is 5.0 x 103. С. Е. G. The x intercept (uM1) in the absence of UTSAone is -0.186. H. The x-intercept (µM) in the presence of UTSAone is -0.188. UTSAone binds to a site other than the active…
The formation of glutamine from glutamate and ammonium ions requires 14.2 kJ mol-1 of energy input. It is driven by the hydrolysis of ATP to ADP mediated by the enzyme glutamine synthetase. {a) Given that the change in Gibbs energy for the hydrolysis of ATP corresponds to ΔG = -31 kJ mol-1, under the conditions prevailing in a typical cell , can the hydrolysis drive the formation of glutamine? (b) What amount {in moles) of ATP must be hydrolysed to form 1 mol glutamine? (c) Suppose that the radius of a typical cell is 10 μm and that inside it 106 ATP molecules are hydrolysed each second. What is the power density of the cell in watts per cubic metre (1W = 1 Js- 1)? (d) A computer battery delivers about 15 Wand has a volume of 100 cm3 Which has the greater power density, the biological cell or the battery?
At 300 K, what fold improvement in a reaction rate do you expect if AG* is brought down from 40 kJ/mol to 20 kJ/mol, without changing of the reaction mechanism, as a result of enzymatic catalysis? е. f. there will be (1) no effect, (2) an increase, or (3) a decrease? The following may or may not be affected by the addition of an enzyme to a chemical reaction. State if A) activation energy of the reaction B) standard free energy of the reaction C) time to reach equilibrium D) equilibrium constant of the reaction E) initial velocity of the reaction g. Remember the simple kinetic mechanism for an enzyme-catalyzed reaction. It was reported that the rate-limiting step is the following reaction k2 ES > P Under these circumstances, the Michaelis constant becomes equivalent to A) [S], when Vo = Vmax B) Turnover number C) Specificity constant D) kcat E) the dissociation constant for the Enzyme-Substrate (ES) complex
The ΔG°′ for hydrolytically removing a phosphoryl group from ATP is about twice as large as the ΔG°′ for hydrolytically removing a phosphoryl group from AMP (−14 kJ · mol−1). Explain the discrepancy.
7.2 Malate dehydrogenase catalyses the reaction: (S)-malate + NAD oxaloacetate + NADH + H* The rate of the forward reaction was investigated in the presence of saturating concentrations of malate and a fixed concentration of enzyme. The following results were obtained: Absorbance (at 340 nm) at timet (minutes) [NAD'] (mmol r") 1 = 0.5 1.0 1.5 2.0 2.5 3.0 1.5 0.033 0.056 0.079 0.102 0.122 0.138 0.036 0.063 0.089 0.040 0.069 0.099 0.128 0.150 0.168 0.043 0.075 0.108 0.140 0.163 0.175 0.047 0.084 0.121 0.158 0.177 0.184 0.052 0.095 0.137 0.180 2.0 0.116 0.138 0.154 2.5 3.33 5.0 10.0 0.192 0.200 Calculate Km and Vmax-
Calculate the standard free-energy change of the reaction catalysed by the enzyme phosphoglucomutase Glucose- 1-P = Glucose-6-P, given that, starting with 28.29 mM Glucose-1-P and no Glucose-6-P, the final equilibrium mixture at 25°C and pH=7.0 contains 9.77 mM Glucose-6-P and the remaining Glucose- 1-P. Give the answer in J/mol.K to one decimal place.
19. The AG, the standard free-energy change, for the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde 3-phosphate (GAP) is +7.55 kJ/mol. The reaction shown below is catalyzed by an enzyme called Triose Phosphate Isomerase (TPI). OH O OH DHAP OH TPI OH M+ OH GAP OH This reaction takes place in glycolysis. At equilibrium, the ratio of GAP to DHAP is 0.0475 at 25°C and pH 7.00. Equilibrium constant, Keq = 0.0475. A) Is the above reaction endergonic or exergonic (going from left to right) under the given experimental conditions? Why? B) Can the above reaction occur spontaneously under the given experimental conditions? Why or why not?

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