QUESTION 2 During glycolysis Glucose-6-phosphate (G6P) is converted to Fructose-6-phosphate (F6P) as shown below. If the standard equilibrium concentrations are: [G6P] = 1.63 M, and [F6P)] = 0.37 M, then Keg' for this reaction is and the reaction is Glucose-6-P → Fructose-6-P O > 1; exergonic O > 1; endergonic O< 1; exergonic O < 1; endergonic
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- P3D.2 In biological cells, the energy released by the oxidation of foods is stored in adenosine triphosphate (ATP or ATP“).The essence of ATP's action is its ability to lose its terminal phosphate group by hydrolysis and to form adenosine diphosphate (ADP or ADP): ATP* (aq) + H,O() → ADP* (aq) + HPO (aq) + H,O*(aq) At pH = 7.0 and 37°C (310K, blood temperature) the enthalpy and Gibbs energy of hydrolysis are A,H =-20kJ mol and A,G=-31 kJ mol", respectively. Under these conditions, the hydrolysis of 1 mol ATP“(aq) results in the extraction of up to 31kJ of energy that can be used to do non- expansion work, such as the synthesis of proteins from amino acids, muscular contraction, and the activation of neuronal circuits in our brains. (a) Calculate and account for the sign of the entropy of hydrolysis of ATP at pH = 7.0 and 310K. (b) Suppose that the radius of a typical biological cell is 10µm and that inside it 1x 10ʻ ATP molecules are hydrolysed each second. What is the power density of…Question:- Two enzymes, acetate kinase and phosphotransacetylase, convert acetate [CH3C(O)O–] and ATP to acetyl phosphate and ADP (acetate kinase reaction) then acetyl phosphate and CoASH (coenzyme A) into acetyl-CoA and inorganic phosphate (Pi ; phosphotransacetylase reaction). What is the ΔG°' for the synthesis of acetyl-CoA from acetate, CoASH, and ATP by this enzyme pair?Question (2rarate nusCollagenase is an endopeptidase that digest native collagen in the triple helix region. The diagram below shows the kinetic plot of collagenase with varied substrate concentration. Plot collagenase activity in response to substrate concentration and find approximate values for Vmax and Km. (please indicate your assumption/s accordingly for this question) 0,04 0,035 0 luM) 0,03 O 200 (uM) 0,025 X 270 (uM) 0.02 A 350 (uMI 0,015 0.01 0,005 On 10 20 30 50 60 Collagenase [pg/ml] Collagenase activity [mM/min]
- 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?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/molQuestion 13 of 40 0% Identify the true characteristic of glutamate at its isoelectric point (pI). 00% The net charge of glutamate is positive. prrect The side chain of glutamate has a negative charge. L00% In an electric field, glutamate migrates toward the anode. orrect The net charge of glutamate is zero. 0% In an electric field, glutamate migrates toward the cathode. 0% Determine the pl of glutamate given its pK at each charge state. Give your answer to two decimal places. Progress Charge: 1+ 1- 2- 0% H,N- CHCO, CH, *H,N-CHCO,H *H,N-CHCO, *H,N–CHCO, CH, CH, pK = 9.67 CH, CH, pK = . = 4.25 0% pk = 2.19 CH, CH, CH, C=0 C=0 C=0 Ć=0 0% MacBook Pro Q Search Default Search &
- Calculate the standard free energy for creatine-phosphate hydrolysis in a cell where [creatine-P]=3 mM, [creatine]=2 mM, and [Pi]= 12.1 mM. Is the reaction exergonic or endogonic?In muscle cells, the AG for glucose+ATP2 glucose-6-P+ADP is –33.5 kJ•mol-'. In contrast, the AG for glucose – 6 – P fructose – 6 - P is –2.5 kJ · mol-1. (a) In a physiological context, which reaction is faster? How do you know? (b) The enzyme that catalyzes glucose + ATP 2 glucose important point of regulation in glycolysis, while the enzyme that catalyzes glucose – 6 – PZ fructose – 6 – P (phosphoglucose isomerase) is not. Why is hexokinase a good step at which to regulate glycolysis relative to phosphoglucose isomerase? 6 – P + ADP (hexokinase) is an | - |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
- Triose phosphate isomerase In a key reaction of glycolysis, dihydroxyacetone phosphate (DHAP) is isomerized into glyceraldehyde 3-phosphate (G3P) by the action of the enzyme triose phosphate isomerase: CH₂OH C=O CH₂OPO3²- DHAP CHO HC-OH CH₂OPO3²- G3P AG°¹ +7.5 kJ/mol Because AG is positive, the equilibrium lies to the left. (a) Calculate the equilibrium constant for this reaction, assuming a temperature of 37 °C. (b) In the cell, depletion of G3P makes the reaction proceed. What is the value of AG if the concentration of G3P is kept at 1/100 of the value of the concentration of DHAP? C ZOOM +Remaining V Ha Question 17 Triose phosphate isomerase catalyzes the conversion of Glyceraldehyde-3- phosphate to Dihydroxyacetone phosphate. Glyceraldehyde-3-P Dihydroxyacetone phosphate The Km of this enzyme for its substrate Glyceraldehyde-3-phosphate is 1.8 x 10 M. When [Glyceraldehyde-3-phosphate] = 30 uM the rate of the reaction (v) was 82.5 umol/mL/sec and the Vmax was 132 umol/mL/sec. Assuming 3 nanomoles/mL of enzyme was used ([Eotal = 3 nanomol/mL) the kcat for this enzyme is: Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a 44000/sec b 1100/sec 88/min d. 120/hour e 11/min Im f 450000/sec g 52800/sec 175/secBegining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq (to one decimal point) of the reaction Pyruvate + NADH+H+ <=> Lactate + NAD+.Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b. please provide a comprehensive explanation with each step taken.