3.Conversion of glucose 6-phosphate to glucose is done by the enzyme glucose6-phosphatase which is present in the liver. Using the Roche Biochemical Pathways, identifyany regulators to this process. (Hint: Read Regulatory Effects in the Legends menu)

Glucose-6-phosphate to glucose conversion is catalysed by the enzyme glucose-6-phosphatase…

Answered: 3. Conversion of glucose 6-phosphate to…

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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select the BEST answer Aconitase is most interesting in that it: Can be coded for by 2 different genes O Exists as either a membrane bound or soluble protein depending on intracellular conditions O Has 2 distinct roles depending on the availability of Iron O Can change the AGº' of it's reaction O Is itself an allosteric regulator of the PDH complex
Two Part Question: A. Which of the following molecules in not a reasonable intermediate in the conversion of oxaloacetate to asparagine? NH3 H2N NH, .o -20,PO COAS A. В. С. HN D. E. В. Glucagon and epinephrine: Promote lipogenesis when systemic energy reserves are low Are secreted when blood glucose levels are high Activate kinases that phosphorylate hormone-sensitive lipase in adipose tissue, which cleaves triacylglycerols to glycerol and fatty acids Activate kinase that phosphorylate acetyl-CoA carboxylase, promotine malonyl-CoA formation Directly activate carnitine transferase A. В. C. D. E.
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…
. Using the principles described in the text regarding pyridoxal phos- phate mechanisms, propose a mechanism for the reaction catalyzed by serine hydroxymethyltransferase.
3. In your textbook the termi- nal enzyme catalyzing the ter- minal step of glycolysis is known as pyruvate kinase (PK). No indication is given that in mammalian tissues there are four different iso- forms of this enzyme. The four mammalian isoforms are known as PKL, PKR, PKM1 and PKM2. PKL is expressed in the liver, and PKR is ex- pressed in red blood cells. C PKM1 and PKM2 are derived from altemative splicing of the PKM gene. PKM1 is a constitu- tively active isoform expressed Active Site A PKM2 Monomer B Fructose-1,6-Bisphosphate N Phe, Ala, Ser Binding Site PKM2 Tetramer "Activator" Binding Site in differentiated cells from various tissues. In contrast, PKM2 has low basal activity and is activated by an effector molecule fructose 1,6-bisphosphate (FBP). PKM2 is expressed in most proliferating cells. In addition, the regulation of PKM2 pyruvate kinase activity plays an essential role in cancer metabolism and is crucial for the growth and survival of cancer cells. Recently, PKM2 has…
5
1.Sustaining intense exercise requires ATP. Could a someone with a defective gene for the enzyme lactate dehydrogenase meet the ATP demand for sustained and intense exercise? Why or why not? Be sure to support your argument with discussion of the metabolic pathways and tissues impacted. 2.Genetic carriers for metabolic diseases (persons heterozygous for a recessive mutation) produce about half the normal amount of the affected enzyme, but rarely exhibit any symptoms or effects. Rationalize this observation, based on your knowledge of the flux and regulation of metabolic pathways.
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.
4. PFK-1 is tightly regulated with multiple potent allosteric regulators. Name three of these regulators and explain how they influence the activity of PFK-1.
b. You conduct some additional experiments to elucidate the starlase metabolic pathway. Your results are shown below. Use this information alongside information from the complementation table above to place the intermediates in the correct order on the pathway. (HINT: use the complementation groups from the table above to help you consolidate information on the tables below. Reference practice question 3 from today's lecture for help). Mutant 1 2 3 4 5 6 Precursor --> [Select] None [Select] Addition to minimal medium starlase + + + + + + --> starlase P + + [Select ] T + O + c. Mutant 2 has a loss-of-function mutation for which enzyme in the starlase synthesis pathway? [Select] E1 E2 E3 E4 Precursor → Intermediate 1 → Intermediate 2 → Intermediate 3 → starlase
3. In your textbook the termi- nal enzyme catalyzing the ter- minal step of glycolysis is known as pyruvate kinase (PK). No indication is given that in mammalian tissues there are four different iso- forms of this enzyme. The four mammalian isoforms are known as PKL, PKR, PKM1 and PKM2. PKL is expressed in the liver, and PKR is ex- pressed in red blood cells. PKM1 and PKM2 are derived from altemative splicing of the PKM gene. PKM1 is a constitu- tively active isoform expressed Active Site A PKM2 Monomer B Fructose-1,6-Bisphosphate N Phe, Ala, Ser Binding Site PKM2 Tetramer "Activator" Binding Site in differentiated cells from various tissues. In contrast, PKM2 has low basal activity and is activated by an effector molecule fructose 1,6-bisphosphate (FBP). PKM2 is expressed in most proliferating cells. In addition, the regulation of PKM2 pyruvate kinase activity plays an essential role in cancer metabolism and is crucial for the growth and survival of cancer cells. Recently, PKM2 has…

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3. Conversion of glucose 6-phosphate to glucose is done by the enzyme glucose 6-phosphatase which is present in the liver. Using the Roche Biochemical Pathways, identify any regulators to this process. (Hint: Read Regulatory Effects in the Legends menu)