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?
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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]
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- MATHEMATICAL What yield of ATP can be expected from complete oxidation of each of the following substrates by the reactions of glycolysis, the citric acid cycle, and oxidative phosphorylation? (a) Fructose-1,6-bisphosphate (b) Glucose (c) Phosphoenolpyruvate (d) Glyceraldehyde-3-phosphate (e) NADH (f) PyruvateLineweaver-Burk plots of enzyme kinetics for the reaction, S <-> P, has the following features: 1/v is zero when 1/[S] equals -40 liter mole^-1; 1/[S] is zero when 1/v equals 2.0 x 10^5 min mole^-1. What are the Vmax and Km? Vmax = 5 umol min^-1, Km = 2.5 mM? Vmax = 5 mmol min^-1, Km = 25 M? Vmax = 5 umol min^-1, Km = 25 mM? Vmax = 5 mol min^-1, Km = 2.5 mM? Vmax = 5 mol min^-1, Km = 25 mM?Lineweaver-Burk plots of enzyme kinetics for the reaction, S <-> P, has the following features: 1/v is zero when 1/[S] equals -40 liter mole^-1; 1/[S] is zero when 1/v equals 2.0 x 10^5 min mole^-1. What are the Vmax and Km?
- Arrange the balanced biochemical equations for all the reactions in the catabolism of glucose to two molecules of glyceraldehyde 3-phosphate (the preparatory phase of glycolysis). First step Last step Answer Bank Fructose 1,6-bisphosphate - dihydroxyacetone phosphate + glyceraldehyde 3-phosphate Fructose 6-phosphate + ATP →→→→ fructose 1,6-bisphosphate + ADP Glucose + ATP → glucose 6-phosphate + ADP Dihydroxyacetone phosphate glyceraldehyde 3-phosphate Glucose 6-phosphate →→→→ fructose 6-phosphatePage 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.molecule A Plot of velocity versus substrate B Lineweaver-Burk plot 1/v Km 1 Vmax (S) Vmx 1 V max 1/2Vmax 1/Vmax -1/Km Km [S] 1/[S] fppt.com molecule Exercise The following data describe an enzyme-catalyzed reaction. Plot these results using the Lineweaver-Burk method, and determine values for KM and Vinax- The symbol mM represents millimoles per liter; 1 mM = 1 × 10 3 mol L. (The concentration of the enzyme is the same in all experiments.) Velocity (mM sec-) Substrate Concentration (тм) 2.5 0.024 5.0 0.036 10.0 0.053 15.0 0.060 20.0 0.061 fppt.com
- What is the catalytic efficiency of Catalase ? Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Carbonic anhydrase Substrate CO2 HCO3 KM (M) 1.2 x 10-2 2.6 x 10-2 Kcat (s-1) 1.0 x 106 4.0 x 105 Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 O A. 4 x 108 M-s-1 O B. 4 x 108 M-1.s-1 OC25x 10-9 M-s1 D. 2.5 x 102 M-1.s-1 OE 1.0 x 107 s1Question: A. To explore the consequences of coupling ATP hydrolysis under physiological conditions to a thermodynamically unfavorable biochemical reaction, consider the hypothetical transformation X⟶Y, for which Δ?′°=20.0 kJ/mol. What is the ratio of [Y]/[X][Y]/[X] at equilibrium? B. Suppose XX and YY participate in a sequence of reactions during which ATP is hydrolyzed to ADP and Pi. The overall reaction is X+ATP+H2O⟶Y+ADP+Pi Calculate [Y]/[X] for this reaction at equilibrium. Assume that the temperature is 25.0 °C and the equilibrium concentrations of ATP, ADP, and Pi are 1.00 M each. C. We know that [ATP], [ADP], and [Pi] are not 1.00 M under physiological conditions. Calculate [Y]/[X] for the ATP‑coupled reaction when the values of [ATP], [ADP], and [Pi] are those found in rat myocytes. Metabolite Concentration in rat myocytes (M) ATP 8.05x10-3 ADP 0.93x10-3 Pi 8.05x10-3Question:- Two enzymes, acetate kinase and phosphotransacetylase, convert acetate [CH3C(O)O–] and ATP to acetyl phosphate and ADP (acetate kinase reaction) then acetyl phosphate and CoASH (coenzyme A) into acetyl-CoA and inorganic phosphate (Pi ; phosphotransacetylase reaction). What is the ΔG°' for the synthesis of acetyl-CoA from acetate, CoASH, and ATP by this enzyme pair?
- Question:: Acyl CoA synthetase hydrolyzes ATP to AMP + PPI (pyrophosphate) as part of the activation of fatty acids to fatty acyl-CoA. Explain the role played by the enzyme inorganic pyrophosphatase in this reaction (in the activation of fatty acids to fatty acyl CoA) in the space provided below.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…Calculate the actual, physiological AG for the reaction Phosphocreatine + ADP = creatine + ATP at 37 °C, as it occurs in the cytosol of neurons, where [phosphocreatine] = 4.7 mM, [creatine] = 1.0 mM, [ADP] = 0.73 mM, and [ATP] = 2.6 mM. Standard Free Energies of Hydrolysis of Some Phosphorylated Compounds Phosphorylated compound AGʻ° (kJ/mol) phosphoenolpyruvate -61.9 phosphocreatine -43.0 ADP (→ AMP + P;) -32.8 ATP (→ ADP + P;) -30.5