Although as a whole, metabolic pathways are thermodynamically favorable, there’s at least one reaction in each pathway that is thermodynamically unfavorable under standard conditions. Provide two different strategies that allow for non-spontaneous reactions to be used as part of an energy-generating pathway.
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Although as a whole,
reaction in each pathway that is thermodynamically unfavorable under standard conditions.
Provide two different strategies that allow for non-spontaneous reactions to be used as part of an
energy-generating pathway.
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- Otto Warburg made an interesting observation in the 1930s about cancer cells using the fermentation pathway to catabolize pyruvate even when the oxygen supply seemed sufficient for oxidative phosphorylation. One modern explanation for this “Warburg Effect” is that it protects the cancer cells from damage from free radicals. Provide a biochemical rationale for this explanation.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?Regulatory enzymes are crucial for the proper functioning and coordination of glycolysis and gluconeogenesis. As a general rule, regulatory enzymes catalyze reactions that are far from equilibrium. Why does this make good biochemical sense?
- How is a “committed step” defined in the context of a metabolic pathway and why are they important? Which steps and/or enzymes are involved in the committed steps in the Krebs Cycle? What are the possible implications of these steps were deregulated?For the following two scenarios, sketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single substrate (S) into product (P), where the reaction is spontaneous in the forward direction. For each of these, overlay the free energy diagram for the uncatalyzed reaction and indicate AAG" on your sketch: a). Substrate binding is rate limiting b). The chemical step is rate limitingA direct measurement of the standard free-energy change associated with the hydrolysis of ATP is technically demanding because the minute amount of ATP remaining at equilibrium is difficult to measure accurately. The value of ΔG′° can be calculated indirectly, however, from theequilibrium constants of two other enzymatic reactions having less favorable equilibrium constants:Using this information for equilibrium constants determined at 25 °C, calculate the standard free energy of hydrolysis of ATP.
- How does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction reaches a maximum value at high substrate?Cells manage to synthesize a variety of seemingly thermodynamically unfavored molecules every day. Phosphorylated glucose is an example of one of these molecules. The direct phosphorylation reaction is depicted below. As indicated, the forward reaction is unfavorable with a positive standard free energy change: glucose + phosphate⇄ glucose-6- phosphate + water ΔG°’ = +14 kJ/mol Describe specifically a thermodynamically favorable route by which the cell can produce glucose-6- phosphate from glucose. Please note cells cannot change either the temperature or the pressure at which the reaction is occurring. Please help me understand by using steps. Thank you!The reaction catalyzed by citrate syn- thase, shown on the right, is the first step of the TCA cycle. In glycolysis, two key reactions to produce ATP occur because an unfavorable reaction is coupled to another reaction that is thermodynamically favorable. The reaction catalyzed by citrate synthase, shown on the right, is similarly coupled to an unfavorable reac- tion in the TCA cycle. Write the unfavorable reaction using structural formulas and write the key step that drives the two coupled reactions forward. What is the overall AG'o of the coupled reactions? CH3-C >=0 + S-COA Acetyl-CoA 0-C-COO- CH₂-COO Oxaloacetate H₂O COA-SH J citrate synthase CH₂-C HỌ—C—COO SO CH₂-COO Citrate AG'= -32.2 kJ/mol
- Quantum tunneling appears to play a significant role in the facilitation of efficient enzyme catalysis in reactions involving the transfer of protons and hydride ions. Provide an energy diagram for a hypothetical reaction in the presence and absence of an enzyme that illustrates the tunneling process.if there are twelve different intermediate products produced in the stage of a metabolic within a cell, we can expect that thereIn some organisms, isoleucine can be synthesized in a multi-step procedure (a series of enzymatic reactions), beginning with a molecule of threonine. Keeping that in mind explain the experimental results below. Amount of endproduct Activity of threonine (isoleucine) deaminase None Low Medium High Very high High Moderate Very low