3. One indication of the relative importance of various ATP-producing pathways is the Vmax of certainenzymes of these pathways. The values of Vmax of several enzymes from the pectoral muscles (chestmuscles used for flying) of pigeon and pheasant are listed below.Vmax (umol substrate/min/g tissue)EnzymePigeonPheasantHexokinase3.02.3Glycogen phosphorylasePhosphofructokinase-1Citrate synthaseTriacylglycerol lipase18.0120.0143.024.0100.015.00.070.01b. Compare oxygen consumption in the two birds.

Pheasant pectoral muscles are clearly anaerobic, as expected from a bird highly trained for…

Answered: 3. One indication of the relative…

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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Similar questions

draw 3 allosteric enzyme curves for glycogen synthesis in the presence of high AMP, high NADH, and no regulators on 1 graph.
8
1. (a) The reaction catalyzed by citrate synthase is the first step of the TCA cycle. In glycolysis, two key reactions to produce ATP occur because an unfavorable reaction is coupled to another reaction that is thermodynamically favorable. The reaction catalyzed by citrate synthase is similarly coupled to an unfavorable reaction in the TCA cycle. Write the unfavorable TCA reaction using structural formulas and write the key step that drives the two coupled reactions forward. What is the overall AG" of the coupled reactions? (b). K(yM) 25.7 Inhibitor Bromoacetyl-CoA ATP NADH 6800 8300 The inhibitor constants for three inhibitors of por- cine citrate synthase are summarized in the table on the right. The compounds were all determined to bind in the ac- tive site as competitive inhibitors of acetyl-CoA. Because they bind as competitive inhibitors, all three inhibitors must exhibit structural similarity to some part of acetyl-CoA. Look up in the textbook the structural formulas for…
The free energy change of each step of glycolysis is given in the table below. ∆G°’ is the free energy under standard conditions (25°C, 1M each reactant, pH 7), while ∆G is the free energy change at presumed physiological conditions. Why must no step have a positive ∆G under physiological conditions?
Allosteric regulation plays a very important role in the regulation of glycogen metabolism. Which of thefollowing is correct? -AMP allosterically inhibits glycogen phosphorylase -Glucose-6-phosphate allosterically activates glycogen synthase -Both A and B -Neither A nor B The value of standard free energy change for reaction A --> B is +3.7 kJ/mol. Under which of thefollowing conditions, the reaction will most likely become exergonic in the direction as written? -Mass action ratio is larger than the equilibrium constant -Couple with ATP hydrolysis -Both A and B -Neither A nor B
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
a particular enzyme catalyzes a single reactant S to a single product P, following michaelis-menten kinetics rp=(VmaxCs) / (Km + Cs) 1. A reaction with this enzyme is carried out at very low substrate concentrations. Draw and label a curve on the plot that describes the reaction kinetics under those conditions.
The glyceraldehyde-3-phosphate dehydrogenase reaction of glycolysis, (glyceraldehyde-3- phosphate → 1,3 bisphosphoglycerate) (Choose all that apply) O conserves energy by transfer of a proton H* to NAD+ forming NADH O has a high energy thioester intermediate on the enzyme/substrate complex O mechanistically uses covalent catalysis O conserves energy in the formation of a oxygen phosphoric ester O conserves energy in the formation of a carboxylic-phosphoric mixed anhydride O mechanistically requires the coenzyme thiamine pyrophosphate (TPP) to act as an electron sink
3. Answer the following questions about the metabolic pathway shown below: glutamate dehydrogenase e NH3 0-C-C-cH2-CH2-C- 0-C-CH-CH2-CH2-C-O + H,O + NAD + NH + NADH + H (a) Label the correct substances as the substrate, enzyme, and co-enzyme. (b) Which of the six classes does the enzyme of this reaction belong to? Why? (c) What is the name of the first molecule in this reaction? (d) Which metabolic pathway is this reaction likely to be a part of? A. glycolysis B. deamination C. beta-oxidation D. fermentation
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…
(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…
Calculate the number of ATPATP generated from one saturated 1212‑carbon fatty acid. Assume that each NADHNADH molecule generates 2.5 ATP2.5 ATP and that each FADH2FADH2 molecule generates 1.5 ATP1.5 ATP .

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