Sketch curves for reaction velocity versus [fructose-6-phosphate] for the phosphorylated and nonphosphorylated forms of PFK-2 in liver.
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- Fructose 1,6-bisphosphatase (FBPase) is a key enzyme in gluconeogenesis. The mammalian enzyme is tetrameric, negatively regulated by both Fructose 2,6-bisphosphate and AMP. Propose three (3) distinct models for how these molecules regulate FBPase activity. Also, describe how the enzyme might differentiate between Fructose 1,6 bisphosphate and Fructose 2,6-bisphosphate binding to the allosteric site on the enzyme with particular emphasis on amino acids comprising the allosteric binding site(s).The mitochondrial form of carbamoyl phosphate synthetase is allosterically activated by N-acetylglutamate. Briefly describe a rationale for this effect.Explain why people with a hereditary deficiency of carnitine acyltransferase II have muscle weakness. Why are the symptoms more severe during fasting?
- Assuming that G6P is labeled at its C1 position, determine where the label will appear in the formed ribulose-5-phosphate from the oxidative stage.From the complete oxidation of glucose (glucose → 6CO2), how many total nucleotide triphosphates are yielded (be sure to deduct payback) as part of substrate level phosphorylation?Fructose 2,6-bisphosphate is a potent stimulator of phosphofructokinase. Explain how fructose 2,6-bisphosphate might function in the concerted model for allosteric enzymes.
- Will the amount of glycogen be higher or lower than normal or unchanged? Pyridoxal phosphate is covalently bonded to glycogen phosphorylase via a Schiff base to Lys 680. What effect would the mutation of Lys680Ala have on the breakdown of glycogen?(This notation means the following: K680 is the normal amino acid in this enzyme. It has been mutated to 680A.) Loss of the gene for the kinase that phosphorylates GSK3 on glycogen synthesis. Effect of the substrate analog below on glycogen synthesis.Predict the effect of each of the following mutants on the rate of glycolysis in liver cells (increase, decrease, no change): (a) Loss of the allosteric site for ATP in PFK-1 (b) Loss of the binding site for citrate in PFK-1 (c) Loss of the phosphatase domain of PFK-2/FBPase-2 (d) Loss of the binding site for fructose-1,6-bisphosphate in pyruvate kinase (e) Loss of acetyl-CoA binding site in pyruvate carboxylaseWhen the identical subunits of chicken liver fatty acid synthase are dissociated in vitro, all of the activities can be detected in the separated subunits except for the β-ketoacyl synthase reaction and the overall synthesis of palmitate. Explain these observations.
- ATP is a (+) allosteric effector, and CTP is a (-) allosteric effector of theenzyme ATCase. Both of these heterotropic effectors bind to the regulatorysubunits on ATCase. The substrates of ATCase, aspartate and carbamoylphosphate, bind the enzyme active site with positive cooperativity (i.e.,they exert a “+” homotropic effect on activity). As the concentrations ofthe substrates change from values where [S] ≪ KM to values where [S] issaturating ([S]≫ KM), how will the binding constants for each of the twoallosteric effectors change? In other words, does ATP bind ATCase withhigher affinity when [S] is low or high? Does CTP bind ATCase with higheraffinity when [S] is low or high?Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different specificities. (a) These proteases are considered serine proteases because the active sites contain serine, histidine and aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing protein substrates. (b) The active site pockets of chymotrypsin, trypsin, and elastase are shown in the image below. Based on the image, which side chain of the amino acids would they prefer to cleave respectively, Ala, Arg, or Trp? Explain your answers. Val 216 Val 190 Asp 189 Chymotrypsin Trypsin ElastaseChymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different specificities. (a) These proteases are considered serine proteases because the active sites contain serine, histidine and aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing protein substrates. (b) The active site pockets of chymotrypsin, trypsin, and elastase are shown in the image below. Based on the image, which side chain of the amino acids would they prefer to cleave respectively, Ala, Arg, or Trp? Explain your answers. Val 216KVal 190 Asp 189 Chymotrypsin Trypsin Elastase