High [ATP] slows glycolysis and speeds of gluconeogenesis because(check all that apply):Pyruvate kinase is allosterically inhibited by low [ATP]PFK-1 is allosterically inhibited by low [ATP]FBPase-1 is inhibited by high [AMP]FBPase-1 is inhibited by low [AMP]Pyruvate kinase is allosterically inhibited by high [ATP]PFK-1 is allosterically inhibited by high [ATP]

ATP is the energy currency of the cell i.e. the cell mostly uses ATP as the source of energy for…

Answered: High [ATP] slows glycolysis and speeds…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 5P

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In muscle tissue, the rate of conversion of glycogen to glucose 6-phosphate is determined by the ratio of phosphorylase a (active) to phosphorylase b (less active). Determine what happens to the rate of glycogen breakdown if a muscle preparation containing glycogen phosphorylase is treated with: (a) phosphorylase kinase and ATP; (b) PP1; (c) epinephrine
Phosphorylase kinase integrates signals from thecyclic-AMP-dependent and Ca2+-dependent signalingpathways that control glycogen breakdown in liver andmuscle cells (Figure Q15–4). Phosphorylase kinase is com-posed of four subunits. One is the protein kinase that cata-lyzes the addition of phosphate to glycogen phosphorylaseto activate it for glycogen breakdown. The other three sub-units are regulatory proteins that control the activity of thecatalytic subunit. Two contain sites for phosphorylation byPKA, which is activated by cyclic AMP. The remaining sub-unit is calmodulin, which binds Ca2+ when the cytosolicCa2+ concentration rises. The regulatory subunits controlthe equilibrium between the active and inactive confor-mations of the catalytic subunit, with each phosphate andCa2+ nudging the equilibrium toward the active confor-mation. How does this arrangement allow phosphorylasekinase to serve its role as an integrator protein for the mul-tiple pathways that stimulate glycogen…
Between your evening meal and breakfast, your blood glucose drops and your liver becomes a net producer rather than a consumer of glucose. Which statements describe the hormone-stimulated process that triggers glucose production by the liver? The increase in (CAMP] causes protein kinase A to phosphorylate pyruvate kinase, thus inhibiting glycolysis in muscle tissue to promote gluconeogenesis in the liver. The decrease in [fructose 2,6-bisphosphate] stimulates FBPase-1, the key enzyme in gluconeogenesis. Epinephrine stimulates an enzyme cascade involving hepatic protein kinase A (PKA) and phosphorylase b kinase, which eventually leads to glycogen breakdown in the liver. O The rapid decrease in blood glucose levels triggers glucagon release by the pancreas. Glucagon stimulates CAMP-dependent phosphorylation of PFK-2/FBPase-2, which decreases [fructose 2,6-bisphosphate]. The decrease in [fructose 2,6-bisphosphate] stimulates PFK-1, the key enzyme in gluconeogenesis.
Which of the following tumor-promoting (oncogenic) proteins promotes increased uptake of glutamine? Group of answer choices Pyruvate dehydrogenase kinase Myc GLUT1 HIF-1 Which of the following has the greatest capacity for ATP production by aerobic respiration? fast twitch muscle slow twitch muscle white fat brown fat Which of the following is an inhibitor of Complex I? Azide UCP1 Catalase Rotenone Which of the following facilitates electron transfer from a 2 electron carrier to a 1 electron carrier? Complex II Complex I Complex III Complex IV
Help fill in the blanks Fructose 2,6-bisphosphate allosterically [inhibits/activates] PFK-1 and allosterically [inhibits/activates] FBPase-1. This is how gluconeogenesis and glycolysis are coordinately regulated. By deduction, glucagon should [inhibit/activate] the enzyme that produces fructose 2,6-bisphosphate since glucagon [activates/inhibits] gluconeogenesis.
ATP is both an inhibitor and substrate of adenyl cyclase. As a substrate, the enzyme converts ATP to cyclic AMP only when the energy sources of cells are low. cAMP mediates the synthesis of a kinase that adds a phosphate to glycogen synthase and phosphorylase. The Km value of the active site is 3.5 x 10-5M while the Km for the allosteric site is 1.7 x 10-3M. What is the implication of the difference in Km value of the active and allosteric site in terms of the utilization of the stored sources of energy of cells? Explain.
Functional and structural analysis indicates that Gleevec is an ATPcompetitive inhibitor of the Bcr-Abl kinase. In fact, many kinase inhibitors under investigation or currently marketed as drugs are ATP competitive. Can you suggest a potential drawback of drugs that utilize this particular mechanism of action?
Phosphorylation can be inactivating or activating. If oxidation of fatty acids is the primary energy supply being used (low insulin, high glucagon), then acetyl COA with rising concentration is being produced independently of PDC. Would PDCK be active or inactive under these conditions? O The kinase will be active The kinase will be inactive Oxidation of fatty acids won't affect PDC O All of the above
The Gq-protein and phospholipase C pathway are responsible for stimulating gluconeogenesis and glycogenolysis. What effect would an agonist or an antagonist have on gluconeogenesis and glycogenolysis?
b) Following this experiment, you would like to elucidate the mechanism of action of pyruvate kinase. Unfortunately, the crystal structure of pyruvate kinase is not available, which requires the enzyme to be modelled based on the available three-dimensional structures of related enzymes. Suggest a bioinformatics approach that can be conducted to perform this study.
What would you expect if a patient carries a mutation in Hexokinase IV (HKIV) that lowers the Km from 10mM to 4mM? O HKIV is still regulated by its product G6P so nothing will change This change is irrelevant since HKIV is only expressed in muscle cells mutant HKIV will have a greater change in reaction velocity in response to change in Glucose levels O mutant HKIV will have a reduced change in reaction velocity in response to change in Glucose levels O Mutant HKIV will always be less saturated by glucose compared to WT HKIV
If intracellular [ATP] = 5 mM, [ADP] = 0.5 mM, and [Pi] = 1.0 mM, calculate the concentration of AMP at pH 7 and 25°C under the condition that the adenylate kinase reaction is at equilibrium.

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