How many ATP is produced in entire oxidation of 1 acetoacetate molecule? Will you get more or less ATPs oxidizing β-hydroxybutyrate?
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Task 1. How many ATP is produced in entire oxidation of 1 acetoacetate molecule? Will you get more or less ATPs oxidizing β-hydroxybutyrate?
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- ACTIVITY 10.4.2 Explain your answer briefly but concisely. What are the steps in the energy investment phase? 2. What are the steps in the energy-yielding phase? 3. What are the enzymes involved in an irreversible reaction? How are these enzymes being activated? What about inhibited? 4. Which step in the glycolytic pathway would ensure that glucose is fated for glycolysis? 5. During strenuous activity, the demand for ATP in muscle tissue is vastly increased. In rabbit leg muscle or turkey flight muscle, the ATP is produced almost exclusively by lactic acid fermentation. ATP is formed in the payoff phase of glycolysis by two reactions, promoted by phosphoglycerate kinase and pyruvate kinase. Suppose skeletal muscle were devoid of lactate dehydrogenase. Could it carry out the strenuous physical activity; that is, could it generate ATP at a high rate by glycolysis? Explain. 6. The transformation of glucose to lactate n myocytes releases only about 7% of the free energy released when…ACTIVITY 10.4.2 Explain your answer briefly but concisely. 1. Why is it that Individuals with thiamin deficiency have high levels of pyruvate in their blood? 2. How would riboflavin deficiency affect the functioning of the tricarboxylic acid cycle? 3. Mammalian liver can carry out gluconeogenesis using oxaloacetate as the starting material. Would the operation of the citric acid cycle be affected by the extensive use of oxaloacetate for gluconeogenesis? Explain your answer.BSC1010C Enzymes & Cellular Regulation Dr. Harris Amylase is an enzyme found primarily in saliva and pancreatic secretions. It catalyzes the breakdown of starch into sugars. A Rate of reaction 0 20 60 40 Temperature, C C Rate of reaction 80 100 B Rate of reaction Enzyme concentration (Substrate concentration always in excess) Substrate concentration (Enzyme concentration constant) The above graphs (A, B & C) provide data on several factors that affect the activity and function of amylase in living organisms. 11. What variables are compared in graph A? What information can be obtained from this data?
- Macmillan Learning Which of the reactions are spontaneous (favorable)? L-malate + NAD+ oxaloacetate + NADH + H+ AG = 29.7 kJ/mol AG = 3.8 kJ/mol DHAP glyceraldehyde-3-phosphate C₂H₂ + H₂ C₂H6 AG = -150.97 kJ/mol glutamate + NAD+ + H₂O NH + a-ketoglutarate + NADH + H+ C6H1309P + ATP C6H14012P2 + ADP AG = -14.2 kJ/mol C₂H₂05 C₂H₂O4+H₂O AG= 3.1 kJ/mol Rh(I) AG = 3.7 kcal/molQuestion:- Explain how the total yield of ATP from the oxidation of 1 mole of glucose to CO₂ + H₂O is affected by the use of the above shuttle versus the use of the Malate Aspartate Shuttle. (above shuttle is glycerol 3-phosphate shuttle)Please answer fast The equilbrium constant (Keq) under standard conditions for the hydrolysis of ATP is 200,000 M. This would suggest the reaction is: 1. proceeding in reverse direction 2. proceeding in forward direction 3. in equilibrium However, this does not take into consideration the concentration of substrates/products within the cell. This is can be calculated by determining the reaction quotient, Q by: [ATP] x [Pi] / [ADP] [ATP] + [Pi] / [ADP] [ADP] x [ATP] / [Pi] [ADP] x [Pi] / [ATP] Biochemical reactions commonly involve the transfer of groups from ATP. What is one of the products of pyrophosphate cleavage from ATP? AMP Adenosine ADP Inorganic phosphate Q5-6. The hydrolysis of ATP is often coupled to other reactions. For example: Phosphoenolpyruvate (PEP) + H2O → Pyruvate + Pi (ΔG'° = -63.1 kJ/mol) ATP + H2O → ADP + Pi (ΔG'° = -30.5 kJ/mol) (The standard free-energy changes for the reactions are indicated in brackets) Q5. Given the information above, what is the…
- HANDOUT C Glucose-6 Phosphate Dehydrogenase and TPI Deficiencies Glucose-6-P GSH + GSH Reduced glutathione 2 H+ NADP+ H₂O₂ Hydrogen peroxide Glucose-6-phosphate dehydrogenase Superoxide radical NADPH + H+ 6-Phosphogluconolactone GSSG Glutathione Oxidized reductase Glutathione peroxidase Aerobic respiration, drugs, fava beans glutathione 2 H₂O Detoxification SOD: superoxide dismutase GPx: glutathione peroxidase HK: hexokinase GSSG and GSH: glutathione, oxidized and reduced forms, respectively CAT: catalase The diagram above gives important details about the HMP shunt. Superoxides/free radicals dis- rupt membrane lipids, causing changes in membrane permeability. The HMP shunt is expressed in liver cells, red blood cells, and in lipid-producing tissues. 1. Discuss how glycolysis is affected in G6PD patients, using the diagrams to explain your response. 2. How does this effect differ from TPI patients? 3. Why are red blood cells, but not the nervous system, affected in G6PD patients?TRUE OR FALSE 1. ADP-ATP is a single path process and is not a cycle. 2. Reaction coupling is a process in which an energetically favorable reaction is directly linked with an energetically unfavorable reaction. 3. Endergonic reaction is the release of energy by breaking chemical bonds of a large reactant and producing smaller products. 4. ATP stands for adenosine triphosphate. 5. Different light intensities can greatly affect the rate of photosynthesis. 6. ADP is composed of a phosphate group, sugar and nucleic acid while ATP does not. 7. Once ATP is used, it will be digested to be used in making other molecules. 8. ATP is an energy carrier. 9. ATP is manufacturers during various processes such as fermentation, cellular respiration, and photosynthesis. 10. Coupled reactions utilizes ADP to facilitate chemical reactions.12020 51.Explain how glutamic acid is oxidized to generate 12020 ATP. 466
- Kinetic Parameters of Enzyme-Catalyzed Reactions TABLE 12-1 The Values of KM, Keat, and Keat/KM for Some Enzymes and Substrates Enzyme Substrate KM (M) 9.5 x 10-5 1.2 x 10-² 2.6 x 10-2 2.5 x 10-2 4.4 x 10-1 8.8 x 10-2 6.6 x 10-4 Acetylcholinesterase Carbonic anhydrase Catalase Chymotrypsin Fumarase Urease Acetylcholine CO₂ HCO₁ H₂O₂ N-Acetylglycine ethyl ester N-Acetylvaline ethyl ester N-Acetyltyrosine ethyl ester Fumarate Malate Urea 5.0 x 10-6 2.5 x 10-5 2.5 x 10-2 Keat (S-¹) 1.4 x 104 1.0 × 106 4.0 × 105 1.0 X 107 5.1 x 10-2 1.7 × 10-1 1.9 X 10² 8.0 x 10² 9.0 × 10² 1.0 X 104 Keat/KM (M¹s¹) 1.5 × 108 8.3 x 107 1.5 x 107 4.0 X 108 1.2 x 10-1 1.9 2.9 × 105 1.6 × 108 3.6 X 107 4.0 X 105 Which enzyme is the most catalytically efficient? Which substrate does chymotrypsin bind to most tightly (assume k_₁ >> K₂)? Is fumarate or malate a better substrate of fumarase? Is it possible to have a kcat/KM of greater than 1 x 10⁹ M-¹ s-¹? Why or why not?Question: Role of the triacyl glycerol cycle. Summarize the cycle referring to Figure 19.9. What role does the cycle play in metabolism? Here are some infromation: Metabolic integration within the human body depends on the redistribution of metabolites, ions, and hormones by the circulatory system. This complex network consists of ∼150,000 km of blood vessels (from major veins and arteries to microcapillaries) that recycle 6 L of blood every minute throughout the body. The circulatory system links together the major tissues and organs of the body in such a way that biochemical pathways in different cells share metabolites, ensuring that the metabolic efficiency of the whole organism is greater than the sum of its parts. This process of maintaining optimal metabolite concentrations and managing chemical energy reserves in tissues is called metabolic homeostasis. This term describes steady-state conditions that apply to a wide variety of physiologic parameters. Metabolic homeostasis is…True of false 6. In glycogen synthesis, the active form of glucose is UDPG. () 7. If people lack thiamine, it can lead to multiple neuritis. () 8. 1mol isocitric acid is transformed into 1mol fumaric acid by TCA cycle, and 7molATP can be produced in the process of electron transfer. () 9. Ketone bodies are harmful products produced during the catabolism of fatty acids. () 10. In the human body, the carbon skeleton for amino acid synthesis can be provided by alpha-ketoacids or other intermediate metabolites during carbohydrate catabolism. In turn, many amino acids can be converted to sugars by the gluconeogenic pathway. ()