4. Which of the following formulations will give the highest ATP yield upon complete oxidation? Show the number of ATPs produced per mole of the compound. Formulation A: o Sucrose o Pyruvate o 1,2,3-tristearoyl glyceride o Oxaloacetate Formulation B: o Maltose o Glyceraldehyde-3-phosphate o Lauric acid o Ala-met-phe-lys-asp
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- Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.33. Which of the following statements is true for the shown reaction? P-O-CH₂ P-O-CH₂ OH A Coo I C=O HOTHS CH₂ Coo A HỌ он D A. The reaction is catalyzed by PFK-1 B. Stimulation of the reaction eventually slows down gluconeogenesis C. Inhibition of glyceraldehyde 3-phopshate dehydrogenase leads to the accumulation of the product B D. All of the above E. None of the above OH 34. Which of the following statements is true for the shown reaction? COO™ CH₂OH HQ -℗ B CH₂ B C-o-℗ + CO₂ A. Insulin can eventually inhibit the reaction B. The reaction only take place in the presence of acetyl-CoA C. The product B is a high-energy molecule, and the next logical step is to use the energy released from B to synthesize ATP D. All of above E. None of the aboveDraw the products of the reaction of xylulose-5-phosphate and erythrose-4-phosphate catalyzed by transketolase in the pentose phosphate pathway. Provide the structure in the protonation state found in physiological conditions. H H H OH FO HO-H H-OH H OPO3²- Q transketolase Draw glyceraldehyde-3- phosphate H H- H H H O OH OH OPO3²- Draw fructose-6- phosphate Q I I
- a What would be the appropriate name for an enzyme that catalyzes each of the following reactions: b H3C iOH OH NH₂ alanine ligase alanine oxidoreductase alanine isomerase alanine transferase OH H3C CH3 H3C NO₂ propanone transferase propan-2-ol hydrolase propan-2-ol oxidoreductase propan-2-ol isomerase OH H3C CH3What is X in the following biochemical pathway? RH NH₂+ A. R CH a-ketoglutarate CH3 coenzyme PLP coenzyme TPP aminotransferase decarboxylase D. glutamate R B. NH X R E. 0 R C. CH CO₂ I OH R. H HTriose phosphate isomerase In a key reaction of glycolysis, dihydroxyacetone phosphate (DHAP) is isomerized into glyceraldehyde 3-phosphate (G3P) by the action of the enzyme triose phosphate isomerase: CH₂OH C=O CH₂OPO3²- DHAP CHO HC-OH CH₂OPO3²- G3P AG°¹ +7.5 kJ/mol Because AG is positive, the equilibrium lies to the left. (a) Calculate the equilibrium constant for this reaction, assuming a temperature of 37 °C. (b) In the cell, depletion of G3P makes the reaction proceed. What is the value of AG if the concentration of G3P is kept at 1/100 of the value of the concentration of DHAP? C ZOOM +
- Complete the balanced equation for the overall reaction. Select answer choice in between brackets. Sucrose + [2 Pi, 4Pi]+[4 ADP, 2 ADP, 4 ATP, 2ATP]+[2 NAD+, 4 NAD+, 6 NAD+]+[H2O, 5 H2O, 3 H2O] --> [2 cirate, 2 oxaloacetate, 2 pyruvate, 2 acetyl-coA]+[4 ADP, 2 ADP, 4 ATP, 2ATP] + [2 NAD+, 4 NAD+, 6 NAD+] + [2H+, 8H+, 6 H+, 4 H+, 10 H+] Does the commercial process require aerated culture medium—that is, is this a fermentation or an aerobic process? A. a fermentation process, because A. niger cells must use O2O2 to continuously regenerate NAD+ B. an aerobic process, because A. niger cells must use O2O2 to continuously regenerate NAD+ C. a fermentation process, because A. niger cells cannot use O2O2 to continuously regenerate NAD+ D. an aerobic process, because A. niger cells cannot use O2O2 to continuously regenerate NAD+19. The AG, the standard free-energy change, for the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde 3-phosphate (GAP) is +7.55 kJ/mol. The reaction shown below is catalyzed by an enzyme called Triose Phosphate Isomerase (TPI). OH O OH DHAP OH TPI OH M+ OH GAP OH This reaction takes place in glycolysis. At equilibrium, the ratio of GAP to DHAP is 0.0475 at 25°C and pH 7.00. Equilibrium constant, Keq = 0.0475. A) Is the above reaction endergonic or exergonic (going from left to right) under the given experimental conditions? Why? B) Can the above reaction occur spontaneously under the given experimental conditions? Why or why not?uizzes/67365/take Based on the image below, select the correct statements. Note: There may be more than 1 correct response. I Ribose 5-phosphate ribose phosphate pyrophosphokinase (PRPP synthetase) glutamine-PRPP amidotransferase adenylosuccinate synthetase AMP > 5-Phosphoribosylamine I adenylosuccinate PRPP lyase 9 steps Adenylosuccinate AMP IMP <-- ADP - AMP <-- GMP <-- IMP IMP dehydrogenase <- GMP - XMP ADP ATP GMP يمد XMP-glutamine amidotransferase Increased levels of ADP inhibit the production of PRPP. Increased levels of GMP inhibit the production of XMP. O Increased ADP activates PRPP synthase to increase PRPP levels. Increased IMP activates glutamine-PRPP amidotransferase to further increase IMP levels. 8 OBC
- His388 Glu357 His388 Glu357 Ring opening Proton HO HO abstraction HO но- G6P He NH- NH His388 His388 His388 Glu357 Glu357 Glu357 HO но HO но- но OH cis-enediol F6P Ring closure intermediate OH Describe the mechanism shown above for phosphoglucose isomerase. Describe the chemistry of each step • How the enzyme appears or might facilitate the chemistry How the enzyme increases the reaction rate.Consider docosanoic acid C12H43CO2H a. Label the alpha and beta Carbons. Show the beta-oxidation in an EXPANDED structure. b. Draw each acyl CoA derived from this fatty acid. c. How many acetyl Co A molecules are formed by complete beta-oxidation? d. How many cycles of beta-oxidation are needed for complete oxidation? e. How many molecules of ATP are formed from the complete catabolism of this fatty acid? Show the complete computation. f. How many moles of ATP per gram of fatty acid is formed from the complete catabolism of the given fatty acid? g. What is the molar mass of the given fatty acid? Solution: Show here the complete computations, [from a to e]The table below shows the purification of liver lactate dehydrogenase. Purification Table of liver LDH Step Crude Extract Ammonium Sulfate DEAE-Sephadex 5'AMP-Sepharose Volume (mL) 200 100 112 40 LDH activity (Units/mL) (mg/mL) [Protein] 47.0 50.00 90.0 63.00 51.0 1.50 137.0/ 0.4 Calculate the LDH yield for the ammonium sulfate step. Provide answer to one decimal only. Show Transcribed Text this is biochemistry and the topic is protein purification could you pleaae show me the full workings even the workings for the comversions