Calculate the factor by which the enzyme will decrease the rate of the reaction with the following information. ES complex releases 30kj/mol of binding free energy that lowers the activaiton energy barrier needed for the transition state.
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Calculate the factor by which the enzyme will decrease the
ES complex releases 30kj/mol of binding free energy that lowers the activaiton energy barrier needed for the transition state.
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- Use the Michaelis-Menten equation to complete the enzyme kinetic data set, when Km is known to have a value of 1 mmol L-1Consider the following data for an enzyme-catalyzedhydrolysis reaction in the presence and absence ofinhibitor I: Using a Michaelis-Menten plot, determine Km for theuninhibited reaction and the inhibited reaction.Draw and label the rate law graph for an allosteric enzyme? Give an explanation for the shape of the curve.
- Sketch on one reaction rate vs. substrate concentration graph & sketch on one Lineweaver-Burk type plot the following:a) A Michaelis-Menten enzyme with a Vmax = 60 1/s and a KM = 125 M.b) An uncompetitive inhibitor of the enzyme described in a).c) An allosteric enzyme with the same Vmax as the enzyme described in a) and follows the sequential modelUse the data below to determine the maximum velocity [in mM/s] of a certain enzyme-catalyzed reaction. v = 0.152 mM/s at [S] = 0.334 mM v = 0.190 mM/s at [S] = 0.450 mMDerive the rate law for the following enzyme reaction chain. Linear the equation you have derived as a Lineweaver-Burk type equation.
- Draw a Gibbs free energy plot for a spontaneous reaction, and then draw how enzymes affect this plot? Do enzymes change (delta)G?Consider the analogy of the jiggling box containing coins that was described on page 85. The reaction, the flipping of coins that either face heads up (h) or tails up (T), is described by the equation h ↔ T, where the rate of the forward reaction equals the rate of the reverse reaction.a. What are ΔG and ΔG° in this analogy? b. What corresponds to the temperature at which the reaction proceeds? What corresponds to the activation energy of the reaction? assume you have an “enzyme,” called jigglase, which catalyzes this reaction. What would the effect of jigglase be and what, mechanically, might jigglase do in this analogy?If the Go for ATP hydrolysis into ADP + inorganic phosphate is 7.3 kcal/mole, and the Go for glutamine synthesis from glutamic acid and NH3 is +3.4 kcal/mole, calculate the average Go for coupling these two reactions (glutamic acid + NH3 + ATP glutamine + ADP + inorganic phosphate
- Sketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single substrate (S) into product (P), where the reaction is spontaneous in the forward direction Overlay the free energy diagram for the uncatalyzed reaction and indicate delta delta G〒 on your sketch: Chemical step is rate limitingWhat is a good estimate of free energy change for formation of an ES complex if the KD for this enzyme/ligand pair is 0.28µM? Give your answer in kJ/molGiven that the standard free-energy change for the reaction glucose + Pi →glucose 6-phosphate is 13.8 kJ/mol, and the standard free-energy change forthe reaction ATP → ADP + Pi is −30.5 kJ/mol, what is the free-energychange for the reaction glucose + ATP → glucose 6-phosphate + ADP?