1/v (mL/Units) y = 2.34x + 0.30 with inhibitor no inhibitor y = 2.34x + 0.20 1/[S] (1/mM)
The Lineweaver-Burk plot was obtained when enzyme inhibition study was done in the absence and presence of 0.50 mM inhibitor. Answer the following questions using correct units and significant figures:
(a) What is the mode of inhibition, competitive, uncompetitive, mixed, or noncompetitive? Explain your answer.
(b) What can you say about the finding site for the inhibitor in relation to the active site of the enzyme? Explain your answer.
(c) Calculate the Km and Vmax in the absence of inhibitor.
(d) Calculate the Km and Vmax in the presence of 0.50 mM inhibitor.
(e) Calculate the KI of the inhibitor using the given equations for reversible inhibition. Which has a higher affinity, the substrate or the inhibitor? How can you tell?
![1/v
(mL/Units)
y = 2.34x + 0.30
with inhibitor
no
inhibitor
y = 2.34x + 0.20
1/[S] (1/mM)](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F5a600697-f443-4c2b-86e3-dc55cb10171e%2Fb373d25a-c5fe-4383-8119-dc03cf7d6486%2Fq6ewfvd_processed.png&w=3840&q=75)
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