Uncompetitive Mixed +Inh +Inh AInh Tnh Anh Anh [S] [S] a. How does the value of Vmax for the enzyme compare to the Vmax "PP of the inhibited enzyme -15

Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
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Data from enzyme inhibition are used to determine a Kmapp and Vmax PP. Comparison of these
values with assays run without inhibitor are used to understand how the inhibition is occurring.
This is useful for better understanding the active site as well as the practical aspect of
pharmaceutical drugs. Below are idealized Line-Weaver Burke plots of different types of
inhibitors.
Comnetitive
Uncomnetitive
Mixed
+Inh
+Inh
4Inh
Anh
Inh
Anh
[S]
[S]
[S]
a. How does the value of Vmax for the enzyme compare to the Vmax PP of the inhibited enzyme
for:
i. Competitive
ii. Uncompetitive
iii. Mixed
b. How does the value of Km for the enzyme compare to the Km PP of the inhibited enzyme for:
i. Competitive
ii. Uncompetitive
iii. Mixed
c. For each situation in Model 1, consider an inhibitor that is better than the one shown on
the graph. Answer the following questions for each type of inhibition:
i. How would the KmPP change?
ii. How would the Vmax PP change?
Transcribed Image Text:Data from enzyme inhibition are used to determine a Kmapp and Vmax PP. Comparison of these values with assays run without inhibitor are used to understand how the inhibition is occurring. This is useful for better understanding the active site as well as the practical aspect of pharmaceutical drugs. Below are idealized Line-Weaver Burke plots of different types of inhibitors. Comnetitive Uncomnetitive Mixed +Inh +Inh 4Inh Anh Inh Anh [S] [S] [S] a. How does the value of Vmax for the enzyme compare to the Vmax PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed b. How does the value of Km for the enzyme compare to the Km PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed c. For each situation in Model 1, consider an inhibitor that is better than the one shown on the graph. Answer the following questions for each type of inhibition: i. How would the KmPP change? ii. How would the Vmax PP change?
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