Choose reaction #6 or #10 in glycolysis and write out the complete reaction. Then, answer the following questions about this reaction. Explain your reasoning for each answer. a. Is it coupled? b. Is it catalyzed by a transferase or an oxidoreductase or neither? c. Is Q > or < or ≈ to K?
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Chemistry
Choose reaction #6 or #10 in glycolysis and write out the complete reaction. Then, answer the following questions about this reaction. Explain your reasoning for each answer.
a. Is it coupled?
b. Is it catalyzed by a transferase or an oxidoreductase or neither?
c. Is Q > or < or ≈ to K?
Step by step
Solved in 2 steps
- Question 2. Answer the following questions: A. The following experimental data was collected during a study of the catalytic activity of anintestinal peptidase with the substrate glycylglycine. Plot the data as a graph, and use it toestimate the Km and the Vmax for this enzyme. B. Now transform this data to plot it as a straight line (Lineweaver-Burk plot). Determine Km andthe Vmax for this enzyme using this new plot. Do your results agree with the estimates made fromthe first graph of the raw data (from 2A)? C. Now assume that the activity of this intestinal peptidase is regulated by covalent modificationof its catalytically active amino acid. Upon phosphorylation, the Km of the catalyzed reaction has been observed to increase by a factor of 3 without any effect on its Vmax. Is the enzyme getting activated or inhibited upon phosphorylation? Justify your answer. D. How will the Lineweaver-Burk plot of the phosphorylated enzyme differ from the plot of the unmodified enzyme (from 2B)?…GAP + Pi + NAD+ ⟹1,3-BPG + NADH (Reaction 1) 1,3-BPG + ADP ⟹ 3-PG + ATP (Reaction 2) Which of the following statements concerning the information above is true? Select all that apply. A.Reaction 2 is an example of substrate level phosphorylation B.These reactions are written in a direction that would indicate gluconeogenesis is occurring in the liver C.The linking of Reaction 1 and Reaction 2 by the intermediate 1,3-BPG is an example of coupling of reactions D.Reaction 1 shows a redox reaction where the carbon skeleton is oxidized to generate electrons for a soluble electron carrier E.These reactions are irreversible under cellular conditionsSuggest the possible class of enzyme (or name of enzyme) for each of theenzyme-catalyzed reactions below. Briefly explain your answer. d. ATP + L-tyrosine + tRNATyr → AMP + PPi + L-Tyrosyl-tRNATyr
- Please answer both parts A.Phosphate-containing compounds, such as ATP, are considered “high-energy” because they have a -ΔGo more negative than -35kJ/mol. Select one: The above statement is TRUE. The above statement is FALSE. B. Which graph(s) display(s) sequential kinetic mechanism of bisubstrate reactions?The following reaction sequence consists of two different substrates catalyzed by an enzyme:let's assume he described his reactions.;E + S1: ES1ES1 + S2: ES1S2ES1S2 → P + Ea.Derive the reaction velocity equation with Michaelis-Menten acceptance.b. Derives the rapid equality of S1 substrate concentration, rather than S2 substrate concentrationsimplify for reaction cards where it is higher.a. Use the values in Problem 23.31 to calculate the energy change in the following reaction. fructose 1,6-bisphosphate + ADP--------> fructose 6-phosphate + ATP b. Is this reaction energetically favorable or unfavorable? c. Write this reaction using curved arrow symbolism. d. Can this reaction be used to synthesize ATP from ADP? Explain.
- Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. Consider that ADP is five times more abundant than AMP. a. Calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. b. Calculate ∆G' for ATP hydrolysis under these conditions (∆G0' for ATP hydrolysis is -32.2 kJ/mol) The energy charge is defined as ( [ATP] + 1/2 [ADP] ) / ( [ATP] + [ADP] + [AMP] )Question 8 of 13 Fill in the blanks: Write C if only statement A is correct, Hif only statement B is correct, E if both statements are correct, M if both statements are incorrect. A. An enzyme catalyzes a reaction by providing an alternative reaction pathway that has a lower energy of activation. B. The enthalpy of the enzyme-catalyzed reaction decreases significantly as compared to the uncatalyzed reaction.KM is determined by measuring the reaction velocity of two enzymes (X and Y) at different concentrations. The curves for X and Y were sigmoid and hyperbolic, respectively. How are these graphs different, and why?
- Question 2 of 13 Fill in the blanks: Write Cif only statement A is correct, Hif only statement B is correct, E if both statements are correct, Mif both statements are incorrect. A. The dissociation of the ES complex to the product is more energetically favored than its dissociation into the separate enzyme and substrate. B. The rate determining step in enzymatic catalysis is the binding of the substrate to the active site of the enzyme.Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.What does the Michalis-Menten equation tell you? A. The velocity of an enzyme under physiological conditions B. The variation of enzyme activity as a function of [substrate] C. The quantity of reactant that disappears per unit time D. A and B E. B and C Vo = Vmax [S] KM + [S] Vo = Vmax® [S] KM + [S]