3. A key step in the biosynthesis of triglycerides is the conversion of glycerol toGlycerol-1-phosphate by ATPglycerol + ATP Oglycerol-1-phosphate + ADPAt steady state in vivo [ATP] = 103 M and [ADP] = 10-4 M. The equilibrium value of theratio [glycerol-1-P] / [glycerol] is 770 at 25° C and pH 7.%3DA. Calculate AG"298K (the standard value of AG at pH 7) and Keg for the reaction aswritten.B. The value of AG°298K for the reaction ADP + P, OUsing this information plus your answer for part (A.), calculate AGO298K and Keg for thereaction|ATP + H,0 is -31.0 kJ mol-1.

Standard Gibbs Free energy at pH 7 (∆G0'298K) is the Gibbs free energy at standard conditions of 1…

Answered: 3. A key step in the biosynthesis of…

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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3.) As mentioned in the March1 outline a critical step in the glycolysis metabolic pathway (conversion for glucose to pyruvate that produces 2 ATP's) is the attachment of dihydroxyacetone phosphate to an isomerase enzyme via an iminium bridge (step1). There is a second step that takes the imine to the enamine that sets up the C-C formation reaction with an enol that you'll cover in two weeks. Show the mechanism for steps 1 (mild acid catalysis) and 2 (draw resonance forms for the iminium cation). In your mechanism, show the intermediate hemiaminal (carbinolamine). Step 2 may address one of the questions asked in Wednesday's class about the water taking out the N-H proton of the iminium cation versus a C-H proton? CH₂OPO3² E-NH₂ + O=C (step 1) CH₂OH Dihydroxyacetone phosphate Iminium (+) cation intermediate (step 2) Enamine (Enol) Intermediate H CH₂OPO32- E-N-C H C. OH H₂O E
Draw the products that would be produced from phospholipase C cleavage of a glycerophospholipid with a phosphoserine head group, an alpha linoleic acid attached to C2 of glycerol and a linoleic acid attached to C, of glycerol. Draw these products at pH=1. Be sure to number the fatty acid carbons in your products.
6. A. List all of the ionizable functional groups that are found in insulin when in aqueous solution. List which amino acid residues have these ionizable groups and list all of the pka and pKb values (including the R groups) that are on both polypeptide chains that make up insulin. (see the table at the end of this HW set; note that tyrosine and cysteine both have unusual pka's, since these side groups ionize above the pKR's given to have a negative charge). B. The isoelectric point of insulin is reported to be around 5.3-5.35. Using the method covered in class, estimate the isoelectric point of insulin and compare your answer to the values above. C. For a polypeptide to be soluble in an aqueous solution, is it good to be near the isoelectric point? Why or why not? Notes: a couple of unusual R group's that ionize (cysteine and tyrosine have R groups that have pka values; histidine has a pkb). The table at the end of this homework set (also in the lecture notes) lists the pka's and…
Please provide an explanation for how to work through this practice problem: Using table 12.1, calculate the free energy change for the synthesis of ATP from cAMP and inorganic phosphate. (Note: cAMP is hydolyzed to AMP, and the free engery of hydrolysis for ATP and ADP is approximately equal.) Table 12.1: (Compound: Change in Free Energy in kJ/mol) cAMP: -50.4 Creatine phosphate: -43.3 ATP: -30.5 Glucose 6-phosphate: -13.9 AMP: -9.2
Triosephosphate isomerase (TIM) catalyzes the conversion of dihydroxyacetone phosphate to glyceraldehyde-3-phosphate. The enzyme’s catalytic groups are Glu 165 and His 95. In the first step of the reaction, these catalytic groups function as a general-base and a general-acid catalyst, respectively. Propose a mechanism for the reaction.
5. Given the following information tables, determine in which cell type cleavage of the terminal phosphate from ADP yields the greatest actual change in free energy. (Please work in kJ/mol.) TABLE 13-6 Standard Free Energies of Hydrolysis of Some Phosphorylated Compounds and Acetyl-CoA (a Thioester) TABLE 13-5 Total Concentrations of Adenine Nucleotides, Inorganic Phosphate, and Phosphocreatine in Some Cells AG (kJimol) (kcalimol) Concentration (MM) Phosphoenolpyruvate 1,3-Bisphosphoglycerate (+3-phosphoglycerate + P) Phosphocreatine -61.9 -14.8 ATP ADP AMP P, PCr Rat hepatocyte Rat myocyte 49.3 -11.8 3.38 1.32 0.29 4.8 -43.0 -103 8.05 0.93 0.04 8.05 28 ADP (+ AMP + P) -32.8 -7.8 -7.3 Rat neuron 2.59 0.73 0.06 2.72 4.7 ATP (+ ADP + P) Location of -30.5 Human erythrocyte 225 0.25 0.02 1.65 ATP (+ AMP • PP) AMP (+ adenosine P) cleavage is important! 45.6 -10.9 E. coli cell 7.90 1.04 0.82 7.9 -14.2 -34 For erythrocytes the concentrations are those of the cytosol (human erythrocytes lack a…
3. 1,3-bisphosphglycerate has a high energy bond that can be used to phosphorylate ADP to make ATP according to the equation below. The free energy of hydrolysis of 1,3- bisphophoglycerate and ATP under standard conditions are -49.4 kJ/mol and -30.5 kJ/mol, respectively. If the [ATP] to [ADP] is about 4 in the cell, how much 1,3-bisphophoglycerate is needed relative to 3-phosphoglycerate to keep this formation of ATP spontaneous? -203PO. H- -OH -OPO3-² + ADP H- -OH -OPO3-² + ATP
84
1. Acid phosphatases are an important group of enzymes that can be detected in human bloodserum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyzebiological phosphate esters as follows:R-O-P-O3-2 + H 2O R-OH + HO-P-O3-2.Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver,and prostrate gland. The enzyme from the prostrate gland is clinically important because anincreased activity in the blood is frequently an indication of cancer of the prostrate gland.Tartrate ion can strongly inhibit the phosphatase from the prostrate gland, but not acidphosphatases from other tissues. How can you use the information above to develop a specificprocedure for measuring the activity of the acid phosphatase of the prostrate gland in humanblood serum?
2. Consider a preparation that contains all of the enzymes and cofactors needed for fatty acid biosynthesis from added malonyl-CoA and acetyl- COA. a. If [2-H) acetyl-CoA (labeled with deuterium) H-c-C-COA and an excess of unlabeled malonyl-CoA are added as substrates, how many deuterium atoms are incorporated into each palmitate? What are their locations in the palmitate structure? (Draw an expanded structural formula for palmitate showing the locations of the deuterium atoms (as drawn in acetyl-CoA above). Explain your answer.
(d) of glucose oxidation in diabetic human patients treated with Metformin (●) and in (nondiabetic) control human patients (0). At –150 min both groups of subjects were started on an intravenous feed of 3-(®H)-glucose, and at t = 0 min they were started on an oral glucose tolerance test whereby a measured amount of glucose in water (a syrupy mixture) was swallowed followed by measure- ment of blood glucose levels at 30 min intervals. The flux of glucose oxidation was measured by the appear- ance of 3H2O in the blood stream. While the information The diagram to the right compares the rate 8000 ORAL GLUCOSE 6000- 4000- 2000- -120 -60 60 120 180 240 300 Minutes cannot be directly extracted from the reaction mecha- nism diagrams in the textbook, the glycolytic step in which the tritium is first released into water is that catalyzed by TPI, as illustrated at the beginning of Question #3. Explain why this step is suitable for measuring the flux of glycolysis through the release of °H…

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