25 Jun You perform a detailed kinetic of an enzyme in the presence and absence of an inhibitor.
Question
MCB100A_F2015_PS9.pages
19. You perform a detailed kinetic of an enzyme in the presence and absence of an inhibitor.
*Figure Attached* The data is shown below. Answer the following questions.
i. Using the plot above, solve for the Vmax and KM of the enzyme without inhibitor and the
apparent V*max and K*M upon addition of inhibitor.
ii. What is the mode of inhibition?
iii. What does this mechanism mean about drug binding with respect to the natural substrates?
1/v (sec/?M)
20. You are working with a homo-oligomeric enzyme and collect the following initial velocity data as a function of substrate concentration, [S].
[S] (mM)
v0
0.5
0.0667
1
0.1
2
0.2
5
0.5
10
1
a. What are the correct units for v0?
Carry out your kinetic analysis by constructing a Lineweaver-Burk plot. Note any special characteristics of your plot. What can you say about the fits of the Km and Vmax parameters?
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