Assuming a eukaryotic cell has complete metabolic ability to fully oxidize glucose(including all metabolic pathways ane necessary organelles).At biochemical level explain the consequence of low oxygen content on all aspects of energy production associated with glucose catabolism.
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Assuming a eukaryotic cell has complete
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- Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.The standard state free energy change for Step 4 of glycolysis (where an aldolase enzyme splits fructose 1,6-bisphosphate into GAP and DHAP) is +23.8 kJ/mol. Yet, glycolysis still proceeds spontaneously in the vast majority of cells. Why does this step in particular proceed spontaneously under typical cellular conditions?In working skeletal muscle under anaerobic conditions, glyceraldehyde 3-phosphate is converted to pyruvate (the payoff phase of glycolysis), and the pyruvate is reduced to lactate. Write balanced biochemical equations for all the reactions in this process, with the standard free-energy change for eachreaction. Then write the overall or net equation for the payoff phase of glycolysis (with lactate as the end product), including the net standard free-energy change.
- 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.Considering the fatty acids: (a) Arachidic acid (C20H40O2); molar mass = 312.5 g/mol) (b) Palmitoleic acid (C16H30O2); molar mass = 256.4 g/mol). How many cycles of β -oxidation are needed for complete oxidation? How many molecules of acetyl CoA are formed from its complete catabolism? How can you calculate the number of molecules (moles) of ATP formed (net) by the complete catabolism of each fatty acid? and the number of moles of ATP formed per gram of each fatty acid metabolized??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.
- . Pyruvate can be processed under anaerobic conditions to ethanol (in yeast) or to lactate (in mammals), as shown. Explain the primary purpose of these reactions. Describe the major biochemical features of each reactionATP is an ALLOSTERIC INHIBITOR of the phosphofructokinase enzyme, which is a key catalyst for one of the first steps of Glycolysis. Citrate (citric acid) is a 6-carbon product of the first reaction of the Krebs Cycle (aka Citric Acid Cycle). Interestingly, Citrate enhances the inhibitory effect of ATP on phosphofructokinase. What is a likely explanation for the inhibitory effects of these molecules? Excess ATP and Citrate signal the cell that Glycolysis should be speeded up. Excess ATP and Citrate signal a positive feedback loop. Excess ATP and Citrate signal the cell that Glycolysis should be slowed. Excess ATP and Citrate compete for the active site of phosphofructokinase.Most individuals with genetic defects in oxidative phosphorylation are found to have relatively high concentrations of alanine in their blood. how this in biochemical terms? please help :)
- When regulating phosphofructokinase, why is there such extensive regulation of this reaction and enzymatic reactions, in general?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?Coupled reactions occur where a nonspontaneous reaction is enabled by coupling it to a spontaneous reaction. This approach is common in biological settings. Determine if ATP could be generated by this biochemical reaction. You have calculated that cell potential is +0.637V. An example of a coupled reaction is the first step of glycolysis, the phosphorylation of glucose to form glucose-6-phosphate shown below. The net ∆Gº for this reaction is