Suppose the biochemical pathway represented in Equation 5-10a is coupled at its first step to the hydrolysis of ATP to ADP. How would this change the expres- sion for AG of the pathway?
Q: HO- HO HN-CO- но-
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- Understanding Enzyme Mechanisms Related to Pyruvate Carboxylase Based on the mechanism for pyruvate carboxylase (Figure 22.3), write reasonable mechanisms for the reactions that follow:If a reaction has a ΔG°′ value of at least −30.5 kJ · mol−1, suffi -cient to drive the synthesis of ATP (ΔG°′ = 30.5 kJ · mol−1), can it still drive the synthesis of ATP in vivo when its ΔG is only −10 kJ · mol−1? Explain.Explain why the coupled reaction ATP → ADP + Pi in the P-class ion pump mechanism does not involve direct hydrolysis of the phosphoanhydride bond.
- Under standard conditions, is the oxidation of ubiquinol (Coenzyme Q) by O2 sufficiently exergonic to drive the synthesis of ATP? If yes, how many ATP can be synthesized assuming 100% efficiency?Show that the free energy change for the succinate dehydrogenase reaction catalyzed by Complex II is insuffi cient to drive ATP synthesis under standard conditions.draw allosteric enzyme curves comparing beta oxidation and fatty acid synthesis in the presence of high AMP and high acetyl CoA, and no regulators
- Whatis the main idea behind the conformational coupling mechanism for ATP synthase? Describe the three conformational states.Do you mean that "reaction themodynamically favorable" is the same as irreversible? PFK-1 conversion of Pyruvate is ADP to ATP, how would you explain this?In a biochemical pathway, three ATP molecules are hydrolyzed. The endergonic reactions in the pathway require a total of 17.3 kcal/mole of energy to drive the reactions of the pathway. What is the overall change in free energy of the biochemical pathway? Is the overall pathway endergonic or exergonic?
- ATP Synthase is known to catalyze the synthesis of ATP with a ΔG°’ close to zero, and a Keq' close to. Why is the value of ΔG°’ different from the known value which is 30.5 kJ/mol (the energy for the reverse of ATP hydrolysis)? If the Keq' value is close to one, how is it ensured that the reaction is driven to the product side and more ATP is obtained?Describe in broad outline the stucture of ATP synthase(what parts make up the molecule and how are these bound in relation to each other? And how this enzyme catalyzes the synthesis of ATP mitochondriaExplain how the position in the active site and function of the oxyanion hole of chymotrypsin supports the theory that enzymes preferentially bind the transition state of the reactions they catalyze