In glycolysis, which step(s) involve(s) isomerization? Check all that apply. 1 2 3 4 ☐ 5 6 07 8 9 ☐ 10 ☐ None of the above
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- Please don't provide handwritten solution ....You are working on an enzyme that obeys standard Michaelis-Menten kinetics. What variable is the V, dependant on if the concentration of the substrate is substantially higher than the concentration of the enzyme? [S] [E] [ES] O [P] O not enough information providedTable 2: Effect of pH on Enzyme Activity pH Absorbance 2 0.05 4 0.35 6 0.8 8 0.5 10 0.4 12 0.1 Use the above data table to complete the following questions: a) Plot the data “pH Vs Abs” using “connect the data point type of graph”. Label the graph with dependent and independent variables where they should be. Provide a title for the graph. b) Over what pH range does catechol oxidase catalyze catechol to benoquinone? c) Explain why the graph has a bell-shaped curve.
- The hydrolysis of sucrose has the following data. Time (min) 0 30 60 90 130 180 [Sucrose] (M) 0.5011 0.4511 0.4038 0.3626 0.3148 0.2674 Sucrose + H₂O → glucose + fructose Unistanit. Determine the half-life. (Use the order from a.) You will need to take into account the order!A multi-enzyme complex Is made up of three polypeptide chains, A, B and C. A is associated with decarboxylase activity; B is a transacetylase, while C is a dehydrogenase. When the protein was placed in a nonpolar solvent, then run in PAGE, two protein bands were observed. Enzyme assays showed that one protein band exhibited decarboxylase activity while the other has both transacetylase and dehydrogenase activities. When the protein was also placed in an aqueous solvent at pH 5.0, then run in electrophoresis, two protein bands were also detected. Further enzyme assays also showed that one protein band exhibits transacetytase activity while the other has both decarboxylase and dehydrogenase activities. a. What types of non-covalent interactions are possible between A, B and C? b. Addition of urea, a reducing agent gave 4 bands in the PAGE profile with a subsequent loss of decarboxylase activity. What could be the reason for the observed result? Explain briefly in terms of the structure…2 3 4 5 B Type here to search 6 7 8 9 10 O O 3 4 5 6 7 8 9 10 pH Level The 11 A researcher investigates the effect of eight different pH levels on the reactions catalyzed by the enzyme catalase. All other factors are held constant. Based on the following graph, what can you conclude about the relationship between the catalase and pH? Reaction Rate by pH Level O T 12 13 optimal (highest) pH level of catalase is 6.5. As the pH level increases, the reaction rate increases. As the pH level decreases, the reaction rate increases. There is no relationship between the pH level and the reaction rate. 14 W 15 16 DELL 17 18 19 20 21 22 → G 23 24 25 3:57 PM 9/15/2022 D D
- One of the examples that we have used to illustrate the concept of equilibrium is the isomerization of glucose-6-phosphate (G6P) to fructose-6-phosphate (F6P), which is the second step in g ycolysis. Draw a graph to show how the reaction Gibbs energy varies with the fraction fof F6P in solution.Label the regions of the graph that correspond to the formation of F6P and G6P being spontaneous, respectively.In biological systems, enzymes are used to accelerate the rates of certain bio- logical reactions. Glucoamylase is an enzyme that aids in the conversion of starch to glucose (a sugar that cells use for energy). Experiments show that 1 pg mol of glucoamylase in a 4% starch solution results in a production rate of glucose of 0.6 ug mol/(mL)(min). Determine the production rate of glucose for this system in the units of Ib mol/(ft³)(day). Ibmol Answer: 0.0639 ft day True FalseWrite the balanced reaction catalyzed by phophoenolpyruvate carboxylase (P PC). Remember to add any cofactors, and to draw the structure formulas (a line-bond representation is fine) for the main substrate and product of the reaction.
- Consider the following mechanism: What kind of reaction is occurring during this step of glycolysis? What metabolite is in Box 1? What metabolite is in Box 2? What metabolite is in Box 3? What enzyme catalyzes this reaction? Circle and label one place on the mechanism where covalent catalysis is occurring. Suggest an amino acid that could fill the role of residue “A” in the mechanism above and draw its structure at pH 7.4. Suggest an amino acid that could fill the role of residue “B” in the mechanism above and draw its structure at pH 7.4. Under standard conditions, this reaction is unfavorable (DG¢° = 23.8 kJ/mol). What conditions in the cell allow for the actual free energy change to be lower (DG » 0), making the reaction readily reversible? Explain your answer. *please help and explain as well as you can*NoneList the 6 major groups of enzymes giving an example of each in the form of an equation.