7. In experimental laboratory, the effect of epinephrine on glycogen mctabolismin a muscle tissue sample of the mutant mice line was studied. After adding6.8. The Metabolism of Ethanol in the Liver307epinephrine to the investigated medium CAMP concentration in the cellsincreased, but glycogen phosphorylase was present only in dephosphorylated,inactive form. Give the enzyme defect most likely in the mutant mice muscles?To solve the problem, answer the questions:a) can these animals perform sudden, intense work, for example, to run awayfrom danger?b) can these animals do moderate physical activity?c) argue the answers by making a scheme of the hormone action on glycogenmetabolism in the muscles.

Epinephrine is also known as adrenaline which is a hormone that is also used as a medication…

Answered: 7. In experimental laboratory, the…

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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Predict the effect of each of the following amino acid substitutions on the KM and kcat of the enzyme-catalyzed reactions
3. Acetylcholinesterase is a serine hydrolase enzyme im- portant in nerve signal transmission, hydrolyzing acetylcho- line, an ester molecule with a positively charged quaternary nitrogen group. The structure of the physiologically relevant substrate of this enzyme is shown on the right. The quater- H₂C nary nitrogen group serves to anchor the molecule in the active site Gly121 Oxy- anion hole Gly122 Ala204 Substrate ACh His447 Catalytic triad Ser203 Glu202 Glu334 Ser229 CH3 N+ CH3 CH3 The a Scale document down rine protease family, consisting of a catalytic triad Ser203- His447-Glu334 with Ser203 supplying the nucleophilic hydroxyl group and an oxyanion hole com- prised of peptide NH groups of Gly121, Gly122, and Ala204, illustrated in the diagram above, for which carbon (green), nitrogen (blue), and oxygen (red) atoms are shown while hydrogen atoms are white. The enzyme catalyzed reaction can be represented by the following scheme: (a)( k1 K2 E + S = ES K-1 K3 EYE + P where ES…
3. Calculate the ATP that is produced when linoleic acid (9,12-octadecadienoic acid; 18:2) is (a) oxidized to CO2 and H20 or (b) converted to the ketone body acetoacetate in the liver and then oxidized to CO2 and H20 in the peripheral tissues. 4. Explain the role of AMP-dependent protein kinase in regulating fatty acid metabolism. What are the ways hormonal control of fatty acid metabolism works between fed and fasted states? Please draw by hand/digitally, schematics showing this regulation in adipose tissue, muscle and liver.
2A. Red blood cells synthesize and degrade 2,3-bisphosphoglycerate (2,3-BPG) by a detour of the glycolytic pathway, as shown below: glyeeraldehyde 3-phosphate GAP dehydrogenase 1,3-bisphosphoglycerate bisphosphoglycerate mutase ADP phosphoglycerate kinase 2,3-bisphosphoglycerate ATP 3-phosphoglycerate 2,3-bisphosphoglycerate phosphatase phosphoglycerate mutase 2-phosphoglycerate (i) The bisphosphoglycerate mutase/2,3-bisphosphoglcerate phosphatase reaction is catalyzed by a single enzyme, BPGM. At alkaline pH, BPGM favors the mutase activity while at lower pH, BPGM favors the phosphatase reaction. Use this information, along with the Bohr effect, to explain in the space below how red blood cells respond to a metabolic defect where a patient experiences chronic, elevated levels of lactic acid. I (ii) Individuals with red blood cell phosphoglycerate kinase deficiency suffer from moderate hemolytic anemia (a condition where red blood cells self-destruct before their normal lifespan). They…
37.Assume that the phosphoryl group in the shown chemical (Phosphoenolpyruvate (PEP)) is labeled with 32P radioisotope. The radioisotope labeled chemical is then allowed to undergo gluconeogenesis in liver cells. Which of the phosphoryl groups in fructose-1,6-bisphosphate are labeled with radioisotope? (Assume that the only fate of the radioisotope chemical is to undergo gluconeogenesis in the liver)a. The phosphoryl group that is attached to the C-1 of fructoseb. The phosphoryl group that is attached to the C-6 of fructosec. Bothd. Neither a nor b
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…
5. Based on your understanding of allosteric regulation and using terminology related to the allosteric (MWC) model, explain how the enzyme glycogen phosphorylase is affected by the binding of AMP and what affect this binding would have on the overall activity of the enzyme. Predict what would happen to the activity of the enzyme when glycogen phosphorylase is covalently modified and there are high levels of ATP in the cell.
(b) the activity of the malate-aspartate shuttle (MAS) system of isolated rat brain mitochondria suspended in an isotonic me- dium buffered to pH 7.4. Diagram A illustrates NADH fluo- rescence emission upon addition of Glutamate in the ab- sence and presence of Aspartate. Diagram B illustrates sim- ilarly NADH fluorescence emission upon addition of Gluta- mate in the presence of Aspartate followed by additions of submicromolar concentrations of Ca2+. As is well estab- lished, the MAS in brain, skeletal muscle, and cardiac mus- Diagrams A and B on the right show changes in Glu A Glu В -No Asp + 0 +0.12 -0.48 + 16 0.81 +1.8 ++ Asp 10 min 2 min cle mitochondria is activated by cytosolic concentrations of Ca2* < 3 µM. To simulate the cytosolic part of the MAS, the following reagents were added to the medium: 4 units/ml glutamate-oxaloacetate transaminase, 6 units/ml malate dehydrogenase, 66 µM NADH, 5 mM aspartate, 5 mM malate, 0.5 mM ADP, 200 nM ruthenium red (to block the mitochondrial…
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2. The precise biochemical mechanisms underlying the rapid shutdown of glycolysis in skeletal muscle upon termination of muscle contraction have remained poorly understood for many decades. It is known that glycolytic flux declines after exercise even though Pi, ADP, and AMP remain high; however, while these adenosine-5'- nucleotides are allosteric activators of phosphofructokinase-1 (PFK-1), this enzyme remains of low ac- tivity despite their presence. The diagrams (A and B) on the right illustrate the increase in the concentrations of glycolytic in- termediates downstream of PFK-1 during exercise for 60 sec followed by the abrupt decline in their concentrations upon ces- sation of muscle contraction. Diagram C shows changes in the concentrations of phosphate metabolites pre- and post-exer- cise. A. Summed concentration of glycolytic intermediates down- stream of PFK-1 (F1,6P2 + DHAP + G3P + GAP + 1,3BPG + 3PG + 2PG + PEP; G3P, glycerol-3-phosphate). B: PFK-1 flux (grey) and the PGK +…
. The allosterically regulated enzyme ATCase binds aspartic acid as a substrate and acylates the a-amino group. Succinate acts as a competitive inhibitor of ATCase because it binds the active site but can't be acylated. The dependence of vo on [aspartic acid] for ATCase is shown in panel (a) of the accompanying figure. Panel (b) shows the effect of increasing [succinate] on v, when [Asp] is held at a low concentration (see thick vertical arrow in panel (a)). Note that in panel (b), vo is not zero when [succinate] =0 (see thin horizontal arrow). Explain the shape of the curve in panel (b). Why does v, increase initially, before decreasing at higher [succinate]? Co0- COO CH2 CH, HC -NH, CH, COO COO Asp Succinate [Asp) [Succinate] [Asp] in experiment b (a) (b)

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