(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)
- Consider 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_forwardENZYME 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_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_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 Two moles of fructose-1,6-biphosphatearrow_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 1. Three moles of glucose-6-phosphate 2. Four moles of pyruvic acidarrow_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 1. Three moles of glucose-6-phosphatearrow_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_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_forwardH. OH co co2 но H co, 1-isopropylmalate 2-isopropylmalate Biosynthesis of leucine involves conversion of 1-isopropyimalate to 2-isopropylmalate (see above). This proceeds in four steps under basic enzymic catalysis via an isolable compound produced in step 2. Write a detailed mechanism for this conversion. Then, draw the intermediate compound) produced in step 2. • You do not have to consider stereochemistry. • Draw uninvolved carboxyl groups in the anionic state, and enolates as carbanions. When needed, abbreviate CoenzymeA-S- as CH3S- In your drawing. aalearrow_forward
- Describe the mechanism of a-chymotrypsin. Explain the roles of constituents of the catalytic triad, their modes of catalysis, and the significance of the oxyanion hole in the catalysis.arrow_forwardStandard redox potentials Eo' for some common compounds in biochemistry: Eo' (Volt) + 0,81 +0,42 + 0,25 12 O₂ + 2 H+ + 2 e NO3 + 2 H+ + 2 e 2 cyt c (ox) + 2 e 2 cyt b (ox) + 2 e Pyruvate + 2 H+ + 2 e* NAD + 2 H+ + 2 e Acétoacétate + 2 H+ + 2 e (2) acétoacétate + NADH + H+ H₂O NO₂ + H₂O 2 cyt c (red) 2 cyt b (red) Lactate (3) 2 cyt c (ox) + 2 cyt b (red) NADH + H+ B-hydroxybutyrate + 0,08 - 0,19 With the help of the above table, determine the spontaneous direction of the following reactions in the standard conditions. Justify your answers by calculating the Gibbs (free) energy of reaction in each case. (1) pyruvate + ß-hydroxybutyrate -0,32 - 0,35 lactate + acétoacétate B-hydroxybutyrate + NAD+ 2 cyt c (red) + 2 cyt b (ox)arrow_forwardIn 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.arrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning