(Answered) 1 you perform a detailed kinetic of an enzyme in the

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1. 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 V_max and K_M 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/μM)

20. You are working with a homo-oligomeric enzyme and collect the following initial velocity data as a function of substrate concentration, [S].

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 K_m and V_max parameters?

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