Given the tri-acylglyceride (TAG) below as source of energy whenadministered from an organism's diet,H,C-OHC-0H,C-o[A] Show the calculated maximum amount of ATP that could begenerated by the full oxidation of the compound. Illustrate where theATPS are derived from (show the reactions and enzymes involved).You can use general structure of the FFA in the reactions involved inthe process.(B) Discuss the fate of the glycerol.(C] One of the FFAS derived from the TAG has the same carbonnumber as glucose. Compare the maximum yield of ATP derivablefrom this FFA as compared to the ATP yield from glucose.

Answered: Image /qna-images/answer/ebcc51b1-f95f-4fef-ac17-f4de1f86596a.jpg

Answered: Given the tr-acyiglyceride (TAG) below…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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What are the amino acids of the catalytic triad of chymotrypsin? State the mode of catalysis shown by each of the amino acids that you have named. (a) (b) Predict what will happen if aspartic acid of the triad is replaced by asparagine. (c) Briefly explain the role of the oxyanion hole for the catalysis of chymotrypsin.
Using Figure 1.3 of the Introduction as an example, a) draw all the structures of the tribasic amino acid lysine involved in the equilibrium reactions that would take place during titration against NaOH, starting with the fully protonated form below (draw the R-group in full). HAN+-CH- COOH (CH2)4 NH°+ b) indicate the numerical pa value of each equilibrium reaction, and which ionizable group is being dissociated in each step. c) indicate the net charge of the amino acid at each step and identify the zwitterion. d) Calculate the pI of this amino acid (show the calculation). e) What would be the predominant ionization states of this amino acid at physiological pH (7.4) and at this pH, what would the ratio of these two states be (show the calculation)?
For each pair of biomolecules, identify the type of reaction (oxidation‑reduction, hydrolysis, isomerization, group transfer, or internal rearrangement) required to convert the first molecule to the second. In each case, indicate the general type of enzyme and cofactor(s) or reactants required, and any other products that would result. A(n) (hydrolysis, oxidation reduction, group transfer, isomerization, internal rearrangment) reaction converts glycerol to glycerol 3‑phosphate. This reaction requires (ADP and a kinase, ATP and a phosphatase, ATP and a kinase, ADP and a phosphatase).
24. Hexokinase catalyzes the phosphorylation of glucose from ATP, yielding glucose-6-P and ADP. The standard-state free energy change for hydrolysis of glucose-6-P is -13.9 kJ/mol. Calculate the standard-state free energy change and equilibrium constant for the hexokinase reaction. AG" for ATP hydrolysis -31.5 kJ/mol
Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…
Write a balanced equation for the complete metabolic oxidation of each of the following. Include O, ADP, and P; as reactants and ATP, CO, and H;0 as products. (a) Stearic acid (b) Oleic acid (c) Palmitic acid (d) Linoleic acid
Write the balanced reaction catalyzed by phophoenolpyruvate carboxylase (P PC). Remember to add any cofactors, and to draw the structure formulas (a line-bond representation is fine) for the main substrate and product of the reaction.
For each pair of biomolecules, identify the type of reaction (oxidation‑reduction, hydrolysis, isomerization, group transfer, or internal rearrangement) required to convert the first molecule to the second. In each case, indicate the general type of enzyme and cofactor(s) or reactants required, and any other products that would result. A(n) (hydrolysis, oxidation reduction, group transfer, isomerization, internal rearrangment) reaction converts glucose to fructose. This reaction is catalyzed by a(n) (dehydrogenase, isomerase, kinase, phosphatase).
B only
Carboxylic acids, such as the one shown below, can be difficult to reduce Provide the name of a reductant A. Explain why this reductant is able to react with the carboxylic acid whereas others cannot (Hint: Draw and discuss the potential reactive intermediates/transition states).
There are parts A-C for this picture included. A) What type of enzyme is Malate Dehydrogenase? choices: Hydrolase, Isomerase, Ligase, Oxideoreductase, Transferase, or Translocase B) Which of the following statements are true in biochemical standard conditions? There can be more than 1. Choices: The reaction is spontaneous since ∆G°' is positive The reaction is spontaneous since ∆G°' is negative The reaction is not spontaneous since ∆G°' is positive The reaction is not spontaneous since ∆G°' is positive The equilibrium favors products since K is greater than 1 The equilibrium favors reactants since K is greater than 1 The equilibrium favors products since K is less than 1 The equilibrium favors reactants since K is less than 1 The reaction is always at equilibrium C) If the concentration of Oxaloacetate is 10^7 times lower than the concentration of Malate D.,Is the reaction Spontanuous? Choices: No, because RTInQ is very positive Yes, because RTlnQ is very…
For each pair of biomolecules, identify the type of reaction (oxidation‑reduction, hydrolysis, isomerization, group transfer, or internal rearrangement) required to convert the first molecule to the second. In each case, indicate the general type of enzyme and cofactor(s) or reactants required, and any other products that would result A(n) (hydrolysis, oxidation reduction, group transfer, isomerization, internal rearrangment) reaction converts glycylalanine to glycine and alanine. This reaction requires (NAD+ and a peptidase or protease, ADP and a phosphatase, H2O and a phosphatase, H2O and a peptidase or a protease)

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