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- Many cancer cells preferentially perform aerobic glycolysis Proliferative tissue 5. Tumor without relying on oxidative phosphorylation to generate energy, a pro- cess known as the "Warburg effect". While less efficient at generating ATP, it has been proposed that the Warburg effect promotes prolifera- tion by generating an abundance of glycolytic intermediates that serve as precursors for other anabolic processes to generate biomass. One consequence of the Warburg effect is that cancer cells that are not bathed in a constant source of fresh glucose – such as cells in a solid tumor that are far from any capillaries (e.g., non-small cell (NSC) lung cancer) – often run out of glucose and activate gluconeogenesis. In this situation, the lactate generated by anerobic glycolysis is converted back to pyruvate to begin gluconeogenesis. or +/-02 Glucose Pyruvate 5% 85% Lactate CO2 (a) matic steps. Beginning with pyruvate, write with words the reaction for the first step, including the name of…6F. What conformational state is stabilized by y in ATP synthase? Why might achieving this state require energy input from the PMF?In the skeletal muscle, in anaerobic conditions, glyceraldehyde 3-phosphate is converted into pyruvate during the payoff phase of glycolysis; and this pyruvate is reduced into lactate during lactic fermentation. Part 1-Write the 11 balanced biochemical equations corresponding to all the reaction steps leading to the conversion of glyceraldehyde-3-phosphate into lactate through glycolysis followed by lactic fermentation. Part 2-Write the net equation of the whole transformation process (i.e. with glyceraldehyde-3-phosphate as the starting substrate; and lactate as the end product).
- Question #7 When you vigorously exercise your muscle cells produce lactate. Ultimately, the lactate that is produced is transported to the liver and converted back into glucose via the gluconeogenesis pathway. 7A Sketch how lactate in the liver is converted into glucose. You do not need to draw any structures of the intermediates, but should provide the names (or acronyms!) of all of the metabolic intermediates involved in the conversion of lactate to glucose. Make sure to indicate points in the pathway that make use of ATP (or an ATP equivalent) and NADH. OH O lactic acid 0000000 A -P=O OH OO во O ⒸO-P=O OH O-P=O O OH OO ОН HO-P=OO OH H OH H O=- 4 pyruvate J OH OH D H -P=O OH fry F OH OH Н. EN VIL O OH OH OH OH N M O LOH K OH OH OH علم OH OH2 The following strain of cells lack one enzyme in metabolic pathway. Which of the following strain can grow on glucose under both aerobic and anaerobic conditions, although it grows slower than normal cells under aerobic condition? Explain (less than 100 words). A strain: lack glyceraldehyde-3-phosphate dehydrogenase B strain: lack lactate dehydrogenase C strain: lack pyruvate dehydrogenase23. An important step in glycolysis is the formation of ATP and pyruvate from phosphoenol-pyruvate (PEP) and ADP. PEP ADP pyruvate+ATP The equilibrium constant (Keq) for this reaction is approximately 2.5x10°. Calculate standard free energy change (AG°') for this reaction. Show your work. onege b. Is the reaction exergonic or endergonic at standard conditions? If, at equilibrium, the concentrations of ADP and ATP are 0.2 mM and 2.0 mM, respectively, what is the equilibrium concentration ratio of [pyruvate] to [PEP]? Show your work. с.
- in human 2. Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout. several medications are used to inhibit the activity of xanthine oxidase and reduce the production of uric acid. You are a biochemist and just discovered a chemical that can inhibit the activity of the human xanthine oxidase. When analyzing its mode of inhibition, you found that the enzyme inhibitor complex requires 450 kJ.mol to dissociate and that it displays kinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministry of health for approval as a medication for gout. Based on the data provided, are they going to authorize it as a medication or not? Explain?phosphorylation/dephosphorylation 5. Diagram the cascade that regulates glycogen metabolism. Please use key enzyme names and arrows to show how glycogen phosphorylase and glycogen synthase are inversely activated/deactivated.4.1 What are the various pathways by which glucose is utilized? 4.2 State the biomedical importance of glycolysis? 4.3 State the irreversible steps in glycolysis? 4.4 State THREE differences between hexokinase and glucokinase ? 4.5 What is glycolysis? What are the rate limiting enzymes of glycolysis?
- Question 2. Answer the following questions: A. The following experimental data was collected during a study of the catalytic activity of anintestinal peptidase with the substrate glycylglycine. Plot the data as a graph, and use it toestimate the Km and the Vmax for this enzyme. B. Now transform this data to plot it as a straight line (Lineweaver-Burk plot). Determine Km andthe Vmax for this enzyme using this new plot. Do your results agree with the estimates made fromthe first graph of the raw data (from 2A)? C. Now assume that the activity of this intestinal peptidase is regulated by covalent modificationof its catalytically active amino acid. Upon phosphorylation, the Km of the catalyzed reaction has been observed to increase by a factor of 3 without any effect on its Vmax. Is the enzyme getting activated or inhibited upon phosphorylation? Justify your answer. D. How will the Lineweaver-Burk plot of the phosphorylated enzyme differ from the plot of the unmodified enzyme (from 2B)?…1. What are the effects of pH and temperature to catalase? What is the optimum pH and optimum temperature for catalase? 2. Explain why the rate of reaction initially increases with increase in temperature then gradually declines as the temperature is further increased. 3. Is the rate of enzymatic reaction always directly dependent on enzyme concentration? Explain. 4. Explain the effect of substrate concentration on enzyme activity. 5. What is the effect of CuSO, on the enzymatic activity of catalase? 6. Is CuSO4 an activator or inhibitor? If it is an inhibitor, what kind of inhibitor is it?GTP or ATP is produced during the conversion of isocitrate into ketoglutarate succinyl CoA into succinate fumarate into malate malate into oxaloacetate