(a)
To determine and explain: The value of
Introduction: Free energy of a system is that amount of energy that is used can be changed into work in a system provided that the temperature and pressure of the system remain the same. It is denoted by
(b)
To determine and explain: The value of
Introduction: Free energy of a system is that amount of energy that is used can be changed into work in a system provided that the temperature and pressure of the system remain the same. It is denoted by
(c)
To determine: How high can the 2PG concentration before the given reaction stops due to
Introduction: Free energy of a system is that amount of energy that is used can be changed into work in a system provided that the temperature and pressure of the system remain the same. It is denoted by
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Becker's World of the Cell (9th Edition)
- Need help, please.arrow_forwardConsider decosanoic acid C12H43CO2H SUB PART TO BE SOLVED How many cycles of beta-oxidation are needed for complete oxidation? How many molecules of ATP are formed from the complete catabolism of this fatty acid? Show the complete computation. How many moles of ATP per gram of fatty acid is formed from the complete catabolism of the given fatty acid? What is the molar mass of the given fatty acid? Solution: Show here the complete computations, [from 1 to 4]arrow_forwardPls help due asaparrow_forward
- ENZYME KINETICS ANALYSIS of 6 Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excess causes gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A student researcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XO which uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct the Lineweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on Table 2 and paste a copy of your Lineweaver-Burk plot. submit the picture of your output in PNG or JPG format. Table 1. Enzyme Kinetic Data Velocity, mM/s [S], mM Хan Kmp Cha 0.492 0.0678 0.0351 0.0615 0.211 0.0531 0.0261 0.0451 0.087 0.0298 0.0157 0.0211 0.048 0.0195 0.0091 0.0142 0.029 0.0127 0.0067 0.0081 Table 2. Enzyme Kinetic Parameters Xanthine Kaempferol Chlorogenic acid Parameters Vmax Км Type of Inhibition Mode of Binding NA NA Lineweaver-Burk Plotarrow_forwardNeed help, please.arrow_forwardNeed help, please.arrow_forward
- Kk149.arrow_forwardWrite balanced biochemical equations for all the reactions in the catabolism of glucose to two molecules of pyruvate (the preparatory & payoff phase of glycolysis), including the standard free-energy change ΔG for each reaction. Then write the overall or net equation of glycolysis, with the net standard free-energy change when one molecule of glucose is converted into 2 molecules of pyruvate.arrow_forwardsub= 18 helparrow_forward
- Saccharides: Using the following substrates, estimate the net ATP yield after glycolytic pathway, Kreb’s cycle and electron transport chain. Assume that the estimate for ATP yield per mole of NADH is 3 moles of ATP, while 1 mole of FADH2 is equivalent to 2 moles of ATP, and one mole of GTP is equivalent to one mole of ATP. Show all pertinent solutions and determine: a) ATP used, b) ATP produced, and c) Net ATP. Based on your solutions, rank the substrates based on increasing yield of ATP Five moles of Acetyl coenzyme Aarrow_forwardSaccharides: Using the following substrates, estimate the net ATP yield after glycolytic pathway, Kreb’s cycle and electron transport chain. Assume that the estimate for ATP yield per mole of NADH is 3 moles of ATP, while 1 mole of FADH2 is equivalent to 2 moles of ATP, and one mole of GTP is equivalent to one mole of ATP. Show all pertinent solutions and determine: a) ATP used, b) ATP produced, and c) Net ATP. Based on your solutions, rank the substrates based on increasing yield of ATP Two moles of fructose-1,6-biphosphatearrow_forwardPage of 6 ZOOM + name: 3. In the last reaction of the citric acid cycle, malate is dehydrogenated to regenerate the oxaloacetate necessary for the entry of acetyl-CoA into the cycle: L-Malate + NAD+ → oxaloacetate + NADH + H* AG'° = 30.0 kJ/mol (a) Calculate the equilibrium constant for this reaction at 25 °C. (b) Because AG°' assumes a standard pH of 7, the equilibrium constant calculated in (a) corresponds to [oxaloacetate][NADH] Keq [L-malate][NAD*] The measured concentration of L-malate in rat liver mitochondria is about 0.20 mM when [NAD*]/[NADH] is 10. Calculate the concentration of oxaloacetate at pH 7 in these mitochondria. (c) To appreciate the magnitude of the mitochondrial oxaloacetate concentration, calculate the number of oxaloacetate molecules in a single rat liver mitochondrion. Assume the mitochondrion is a sphere of diameter 2.0 microns.arrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning