Ans: This reaction is consist of two half reactions. First one is the conversion of ADP into ATP and second one is the conversion of X into Y. So the net DG for the overall reaction is the sum of DG for these two half reactions.
Now DG for conversion of ADP into ATP at standard condition is 30.5 KJ/mol, so the DG for the conversion of X into Y is equal to 57.3-30.5, which is 26.8 Kj/mol.
Now in living cell the DG for ADP to ATP conversion is 57 KJ/mol. So if that's the case than the free energy change for the conversion of X into Y is equal to 0.3 KJ/mol.
So the answer is one of the two i described above.
Consider the following reaction: X + ADP > Y + ATP If the net DG for...
4. Consider the following reaction: ATP + pyruvate phosphoenolpyruvate + ADP Given: Standard free energy of hydrolysis for ATP to ADP is -30.5 kJ/mol Standard free energy of hydrolysis for phosphenolpyruvate to pyruvate is -61.9 kJ/mol Calculate AGⓇ and Key for this reaction.
Consider the hydrolysis of ATP: ATP(aq) + H2O(l) → ADP(aq) + Pi(aq). This reaction has ΔH°= −24.3 kJ/mol and ΔS°= +21.6 J/mol-K. The actual concentrations of ATP, ADP, and Pi are not 1 M in a biological cell. How much energy can the conversion of ATP to ADP supply when it occurs at physiological conditions in E. coli where the temperature is 37°C and the approximate concentrations are ATP = 11.2 mM, ADP = 1.52 mM, Pi = 20.0 mM?...
Consider the following reaction:
Glucose + ATP ↔Glucose -6-phosphate + ADP
Using the information in the below determine Go for
this reaction and comment on the spontaneity of this reaction.
What the information does the Go parameters in the
table below provides about the rate of the ATP hydrolysis.
Below is the structure of glucose-6-phosphate. Identify which
anomer does it represent?
Standard free energies of hydrolysis of some
phosphorylated compounds
compound
Go (kJ mol-1)
ATP (to ADP)
-30.5
pyrophosphate
-19.3...
The reaction for the hydrolysis of ATP is: ATP rightarrow ADP + Pi + 7.3kcal Is this an endergonic or exergonic reaction and why? Draw a reaction energy diagram for this reaction (do not need to include specific numbers) and label: X and Y axis, reactants, products, transition state, energy of activation. Draw an additional curve on your diagram above (use a dotted line or another color to distinguish) to indicate how the progress of reaction would be affected by...
Question 11 1 pts Consider the hydrolysis of ATP: ATP(aq) + H2O(1) - ADP(aq) + P(aq). This reaction has AH°= -24.3 kJ/mol and AS - +21.6 J/mol-K. The actual concentrations of ATP, ADP, and Pi are not 1 Min a biological cell. How much energy can the conversion of ATP to ADP supply when it occurs at physiological conditions in E.coli where the temperature is 37°C and the approximate concentrations are ATP - 14.8 mM, ADP - 3.65 MM, P,...
Consider the following reactions: #1: ATP + H2O -> ADP +P, #2: Phosphocreatine + H20 — #3: Phosphocreatine + ADP — creatine + P creatine + ATP (AG" =-31 kJ/mol) (4Gº = -43 kJ/mol) (AG'= -12 klimol) AG" for reaction #3 would be 12 km 0-12 kJimo 0 -43 kJimo 0 74 klimo
Add coefficients to the reaction summary to show the net results of glycolysis. glucose+? ADP+? Pi+? NAD+⟶? pyruvate+? ATP+? NADHglucose+a ADP+b Pi+c NAD+⟶x pyruvate+y ATP+z NADH You do not need to add the water and hydrogen ions necessary to balance the overall reaction. Then, Draw the structure of pyruvate at pH 7.4.
2. For the following reaction: ATP+ creatine + H2O creatine phosphate + ADP + P, The relevant half reactions are: ATP → ADP + Pi Creatine phosphate + H2O-> creatine AG-30.5 kJ/mol ΔG°,--43.1 kJ/mol a. (2 pts.) Calculate the ΔG°, for the overall reaction. b. (2 pts.) Is the reaction spontaneous or non-spontaneous? Endergonic or exergonic?
The reaction catalysed by pyruvate kinase is: K'eg 3.63 x 105 Phosphoenolpyruvate + ADP -> pyruvate ATP a) Calculate the AG°" for this reaction. Show your working. 3 marks b) The hydrolysis of ATP has following equation: ATP+H20ADP P AG-30.5 kJ/mol Calculate the AG" for the following reaction: Phosphoenolpyruvate -> pyruvate Pi Show your working. 2 marks c) At 37 °C, the steady-state concentrations of phosphoenolpyruvate, ATP, and ADP have been measured to be 23 μΜ, 1.85 mM and 140...
Hexokinase catalyzes the following reaction in glycolysis: Glucose + ATP ← → glucose-6-phosphate + ADP The standard free-energy change for this reaction in the direction written is -16.7 kJ/mol. The concentrations of the related reaction components in the hepatocyte of a mammalian cell are: Glucose: 6 mM Glucose-6-phosphate: 0.074 mM ATP: 1.00 mM ADP: 0.25 mM What is the actual free-energy change for the reaction at body temperature (37 C)?