7. A thumb on the balance. The reaction catalyzed by phos- phorylase is readily reversible in vitro. At pH 6.8, the equi- librium ratio of orthophosphate to glucose 1-phosphate is 3.6. The value of AG°' for this reaction is small because a glycosidic bond is replaced by a phosphoryl ester bond that has a nearly equal transfer potential. However, phospho- rolysis proceeds far in the direction of glycogen breakdown in vivo. Suggest one means by which the reaction can be made irreversible in vivo.
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- Energetic of Fructose-1 ,6-bis P Hydrolysis (Integrates with Chapter 3.) The standard free energy change (G) for hydrolysis of fructose-1. 6-bisphosphate (FBP) to fructose-S-phosphate (F-6-P) and P: is -16.7 KJ/mol: FBP + H2O fructose-6-P + Pi The standard free energy change (G) for ATP hydrolysis is -30.5 KJ/mol: ATP + H2O ADP + Pj What is the standard free energy change for the phosphofructokinase reaction: ATP + fructose-6-P ADP + FBP b. What is the equilibrium constant for this reaction? c. Assuming the intracellular concentrations of [ATP] and (ADP] are maintained constant at 4 mM and 1.6 mM, respectively, in a rat liver cell, what will be the ratio of [FBP]/[fructose-6-P] when the phosphofructokinase reaction reaches equilibrium?ATP yield. Each of the following molecules is processed by glycolysis to lactate. How much ATP is generated from each molecule?Serine protease enzyme mutation To show differences in the effect of the nucleophilic attack of the carbonyl group (C=O) of peptide bond between the catalytic triad of serine, histidine and aspartic acid, and another catalytic triad contains alanine, histidine and aspartic acid Provide/ draw an example of catalytic mechanism with catalytic triad contains alanine, histidine and aspartic Please answer completely will give rating surely
- Help filling in the blanks: Pyridoxal phosphate, PLP, is produced from pyridoxine or vitamin B6. PLP is considered a/an [1C/2C/acyl/amino/carboxyl] carrier. In transaminases, PLP forms a [Schiff base/acetal/phosphoanhydride/condensation] with an amino acid and causes the [a- amino/a-carbon/a-carboxyl] to become [electrophilic/nucleophilic] allowing replacement of the amino group on the amino acid with a ketone. PLP is also used by several other enzymes that work on amino acids because in forming a covalent bond with amino acids it provides for an opportunity for nucleophilic attack and because PLP is conjugated, the cofactor is able to [delocalize/transfer/reduce/stabilize] pi electrons in the substrate and thus [stabilize/delocalize/transfer/reduce] the transition state of the reaction. Production of citrulline occurs in the [cytosol/mitochondrial matrix] while the rest of the urea cycle occurs in the [cytosol/mitochondrial matrix]. Urea is produced in the…Working at cross-purposes? Gluconeogenesis takes place during intense exercise, which seems counterintuitive. Why would an organism synthesize glucose and at the same time use glucose to generate energy?25. An ATP saved is an ATP earned. The complete oxidation of glucose 6-phosphate derived from free glucose yields 30 molecules ATP, whereas the complete oxidation of glucose 6- phosphate derived from glycogen yields 31 molecules of ATP. Account for this difference.
- Glycerophospholipids Phosphatidylethanolamine 3. In case the cell is in a state requiring large amount of ATP to support energy-requiring reactions/pathways, assuming that you have 1 mole of each of the said lipids are catabolized and complete oxidized, will the total net ATP yield from these two lipids be higher or lower than the sum of the net ATPs generated from each fatty acid components? Justify your answer in biochemical terms and using 5 sentences or less.MULTIPLE CHOICE In patients with Lesch Nyhan Syndrome, purine nucleotides are overproduced and over excreted. The hypoxanthine analogue Allopurinol, which effectively treats gout , has no effect on the severe neurological symptoms of Lesch- Nyhan patients because it does not A. decrease de novo pyrimidine synthesis B. decrease de novo purine synthesis C. decrease urate synthesis D. increase PRPP levels (Phosphoribosyl pyrophosphate)Lysozyme’s use of aspartic acid and glutamic acid, to break the glycosidic bonds of the eubacterial cell wall (composed of peptidoglycan), illustrates the common enzymatic pattern of: hydrolysis (catabolic), using nonpolar amino acids at the active site hydrolysis (catabolic), using polar amino acids at the active site condensation (anabolic), using nonpolar amino acids at the active site condensation (anabolic), using polar amino acids at the active site all of the above
- 6. Cycle of tricarboxylic acids (TCA):• importance for cellular metabolism;• intracellular localization of TCA enzymes;• sequence of TCA reactions;• TCA enzymes and coenzymes;• substrate phosphorylation reactions in TCA;• decarboxylation reactions in TCA;• enzymes and coenzymes in dihydrogen reactions in TCA;• mechanisms of regulation of TCA.The reaction catalyzed by phosphorylase is readily reversible in vitro. At pH 6.8, the equilibrium ratio of orthophosphate to glucose 1-phosphate is 3.6. The value of ΔG°’ for this reaction is small because a glycosidic bond is replaced by a phosphoryl ester bond that has a nearly equal transfer potential. However, phosphorolysis proceeds far in the direction of glycogen breakdown in vivo. Suggest one means by which the reaction can be made irreversible in vivo.Glycerophospholipids Phosphatidylethanolamine 2. Calculate the net ATP yield per fatty acid after complete oxidation. Show your solution using a table of pathways, reducing equivalents, and ATP