Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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The phosphoryl group transfer potentials of phosphorylated compounds with high hydrolysis values are substantial.
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- The phosphorylation and oxidative decarboxylation of oxaloacetate by inorganic phosphate (Pi) to make phosphoenolpyruvate and carbon dioxide is endergonic under intracellular conditions. It is characterized by this equation: Oxaloacetate + Pi ←→ Phosphoenolpyruvate + H2O + CO2 ΔG’ = +24.6 kJ/mol The synthesis of GTP from GDP and inorganic phosphate (Pi) in solution is endergonic under intracellular conditions, and it is characterized by this equation: GDP + Pi ←→ GTP + H2O ΔG’ = +30.5 kJ/mol Write a new net thermodynamically coupled reaction equation that describes the synthesis of phosphoenolpyruvate from oxaloacetate using the hydrolysis of GTP to power the reaction and calculate the new net ΔG’ of this reaction. Show all of your work.arrow_forwardPhosphorylated molecules with high _____________ values of hydrolysis have large phosphoryl group transfer potentials.arrow_forwardFree energy changes under intracellular conditions differ markedly from those determined under standard conditions. AG" =-30.5 kJ/mol for ATP hydrolysis to ADP and P,. Calculate AG for ATP hydrolysis in a cell at 37 °C that contains [ATP] =3 mM, [ADP] =1mM, and [P] =1 mM.arrow_forward
- Calculate the ATP yield for the full catabolism of a phospholipid containing ethanolamine, C18:3 Δ9, 12, 15 and oleic acid. Include any ATP “expenses” or “income”. This will be a complex problem—neatly show your work and justify your choices.arrow_forwardThe primary source of phosphate for chemical reactions in cells comes as ATP, ADP, or AMP. The ΔG˚’ for the hydrolysis of ATP into ADP and Pi is -30.5 kJ/mol. Calculate the equilibrium constant for the hydrolysis of ATP.arrow_forwardGlucose-1-phosphate has a higher phosphoryl group transferpotential than does glucose-6-phosphate. Review the structures of these molecules and suggest a reason for thisphenomenon.arrow_forward
- b) Why might the compound shown below act as a transition state analog of phosphoglucose isomerase? A drawing of the normal transition state for this enzyme is needed. HO- OH T .N -OH -OH CH₂OPO₂²-arrow_forwardWhat is the relationships between Kcat and that of stability. How is Kcat related to activation energy?arrow_forwardTriose 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 +arrow_forward
- In many biochemical reactions which involves the formation of an enolate intermediate, the carbonyl oxygen of the substrate is coordinated to a divalent metal ion (usually zinc or magnesium) in the active site. Explain with structural drawings, how this ion-dipole interactions affect the acidity of the a-protons?arrow_forwardCalculate the equilibrium constant for the reaction glucose-1-phosphate + H2O → glucose + H2PO4− at pH 7.0 and 25°C (ΔG°′ = −20.9 kJ · mol−1).arrow_forwardThe free energy released by the hydrolysis of ATP under standard conditions is −30.5 kJ/mol. If ATP is hydrolyzed under standard conditions exceptat pH 5.0, is more or less free energy released? Explain.arrow_forward
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