Discuss the metabolic rationale for phosphorylation of acetyl-CoA carboxylase by AMP-activated protein kinase (AMPK) and cyclic AMP-dependent protein kinase (PKA).
Q: Briefly describe the biological rationale for each of the following allosteric phenomena: (a)…
A: Allosteric regulation occurs when an enzyme's activity is affected by binding of a small molecule.…
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Q: Discuss the metabolic rationale for phosphorylation of acetyl-CoA carboxylase by AMP-activated…
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- Discuss the metabolic rationale for phosphorylation of acetyl-CoA carboxylase by AMP-activated protein kinase (AMPK) and cyclic AMP–dependent protein kinase (PKA).The serine residues in acetyl CoA carboxylase that are the target of the AMP-activated protein kinase are mutated to alanine. What is a likely consequence of this mutation?Inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG) are second messenger molecules derived from the cleavage of phosphatidylinositol 4,5-bisphosphate [PI(4,5) P2] by activated phospholipase C. Describe the role of IP3 in causing a rise in cytosolic Ca2+ concentration. How do cells restore resting levels of cytosolic Ca2+? What is the principal function of DAG?
- Describe the general function and structural features of G-protein-coupled receptors (GPCRs). Be sure to include an explanation of GTPase activating proteins (GAPs) and GDP exchange factors (GEFs) in the context of the GTPase cycle. How are different classes of heterotrimeric G-proteins defined?Explain the indirect effect that allosteric effectors have on pyruvate dehydrogenase activity through phosphorylation/dephosphorylation of components within the PDH-complex.Determine the specific types of mutations in the gene for the regulatory subunit of cyclic-AMP-dependent protein kinase (PKA) that could lead to either a permanently active PKA or a permanently inactive PKA.
- 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?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.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
- Considering the gluconeogenesis that may occur after removal of the amino group from amino acids, will malate be an intermediate in all such metabolic routes between amino acids and glucose? Explain. The phosphoenolpyruvate carboxykinase (PEPCK) gene is more actively transcribed when glucagon is present in blood. Putting the signal cascade responsible for that activation aside for the moment, will the reaction that PEPCK mediates be in zero or first order for that increased transcription to have a maximal affect on gluconeogenesis? Explain.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.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…