Given the active site diagram below, which of the indicated components is/are necessary for proton shuttling? O.... NH+ -~ 2 +H₂N HN NNH Mn²+ O 03 5 1 and 5 1 Mn²+ 2 3
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- Assume that an enzyme-catalyzed reaction follows the scheme shown: E + S ES E + P k₁ = 1 x 10%/M-s k-1 = 2.5 x 10%/s k2= 3.4 x 107s What is the dissociation constant for the enzyme-substrate, Ks? What is the Michaelis constant, Km, for this enzyme? What is the turnover number, Kcat, for this enzyme? What is the catalytic efficiency for the enzyme? If the initial Et concentration is 0.25mM, what is Vmax?The protein catalase catalyzes the reaction 2H,O,(aq) — 2H,O(l) + O,(g) and has a Michaelis-Menten constant of KM = 25 mM and a turnover number of 4.0 × 107 s¯¹. The total enzyme concentration is 0.010 µM and the initial substrate concentration is 4.83 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax) for this enzyme. Rmax Calculate the initial rate, R (often written as V), of this reaction. R = ×10 mM.s-1 mM-s-1Explain why the coupled reaction ATP → ADP + Pi in the P-class ion pump mechanism does not involve direct hydrolysis of the phosphoanhydride bond.
- Given the following information, calculate the catalytic efficiency of the enzyme. Step by step please [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμMThe protein catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide:2 H2O2 (aq) → 2 H2O (l) + O2 (g)and has a Michaelis-Menten constant of 25 × 10-3 mol·dm-3 and a turnover number of 4.0×107s-1.The total enzyme concentration is 0.016×10-6 mol·dm-3 and the initial substrate concentration is4.32×10-6 mol·dm-3 Calculate the maximum reaction rate (????) for this enzyme, and the initial rateof this reaction. Note that catalase has a single active site.If a 0.1 M solution of glucose 1- phosphate at 25 °C is incubated with a catalytic amount of phosphoglucomutase, the glucose 1-phosphate is transformed to glucose 6-phosphate. At equilibrium, the concentrations of the reaction components are Calculate Keq and ΔG′° for this reaction.
- The active site of an enzyme that uses a general acid-base catalytic mechanism contains a Glu and an Asp residue (both of which are essential for catalysis) with pKa values of 5.9 and 4.5, respectively. If the enzyme is found in the lysosome (pH = 5.2), which residue will act as the general acid and which will act as the general base during the initial steps of the reaction?Discuss the relationship between redox potentials E0’ and the organization of the components of the electron transport chain. Be specific, i.e., use data/actual values to back up your discussion. a) What are the values of E0’ for all the components of the ETS? b)How are the E0’ related to ∆G values? c) How do the values of E0’ vary among the participants in the ETS relative to their position in the ETS?At what substrate concentration would an enzyme with a kcat of 25.0 s-1 and a KM of 3.5 mM operate at 25% of its maximal rate? How many reactions would the enzyme catalyze in 45 seconds when it is fully saturated with substate, assuming the enzyme has one active site?
- 10) The phosphorylation of glucose is an unfavorable reaction, with ΔG°’ = 13.8 kJ/mol. We can couple this to the favorable reaction of ATP hydrolysis to make the overall process favorable. a) Describe how this works. b) If ΔG°’ for ATP hydrolysis = -32.2 kJ/mol, what is the overall ΔG°’ of the reaction?Many metabolites are maintained at steady-state concentrations that are far from equilibrium. A comparison of Kéq and Q, the mass-action ratio, can determine whether a metabolic reaction is far from equilibrium. The equation for this equilibrium is, fructose 6-phosphate + ATP = fructose 1,6-bisphosphate + ADP Calculate Kg for this reaction at T = 25.0 °C. Ka 1.8 x10-6 AG' = -14.2 kJ/mol Incorrect Calculate the mass-action ratio, Q, from the approximate physiological concentrations for rat heart tissue shown in the table. Metabolite Concentration (µM) Q = 3 fructose 6-phosphate 81.0 fructose 1,6-bisphosphate 15.0 Incorrect ATP 12,500 ADP 1,340How would chymotrypsin's catalytic triad be affected by extremely low and extremely high pH values (assuming the rest of the protein remains intact)?