4. The following rate constants have been determined for a Michaelis –Menen enzyme: ki = 2.5 x 10$ M' s', k.1 =2 x 10³ s', and k2= 5 x 10ª s'. a. Calculate Ks and Km for this enzyme. b. Does the substrate binding approach equilibrium or the steady state? Explain why.

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4. The following rate constants have been determined for a Michaelis -Mena enzyme: kı = 2.5 x
10$ M' s', k.1 = 2 x 103 s!, and k2= 5 x 10* s'.
%3D
a. Calculate K, and Km for this enzyme.
b. Does the substrate binding approach equilibrium or the steady state? Explain why.
c. In a 500ul reaction containing 2pmol of the enzyme and saturating levels of substrate.
What is the Vmax for the enzyme? Assume two active sites per enzyme molecule.
d. What substrate concentration would be needed for the reaction in 4c to achieve half
maximal velocity? Justify your answer mathematically.
e. What is the efficiency of this enzyme? Would this enzyme be considered a perfect
enzyme? Explain.
Transcribed Image Text:4. The following rate constants have been determined for a Michaelis -Mena enzyme: kı = 2.5 x 10$ M' s', k.1 = 2 x 103 s!, and k2= 5 x 10* s'. %3D a. Calculate K, and Km for this enzyme. b. Does the substrate binding approach equilibrium or the steady state? Explain why. c. In a 500ul reaction containing 2pmol of the enzyme and saturating levels of substrate. What is the Vmax for the enzyme? Assume two active sites per enzyme molecule. d. What substrate concentration would be needed for the reaction in 4c to achieve half maximal velocity? Justify your answer mathematically. e. What is the efficiency of this enzyme? Would this enzyme be considered a perfect enzyme? Explain.
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