Enzyme X follows Michaelis-Menten kinetics. You add an inhibitor to your enzyme and you notice that the Vmax has decreased while the Km for enzyme X has increased as a result of adding the inhibitor. What are you able to conclude from this information? The inhibitor must be competitive The amount of total enzyme available to catalyze the reaction in the presence of the inhibitor has likely decreased The enzyme has a higher affinity for its substrate in the presence of the inhibitor The substrate concentration required to reach 1/2 of the maximum velocity for this enzyme has increased as a result of the inhibitor More than one of the above are conclusions that can be drawn from this information
Enzyme X follows Michaelis-Menten kinetics. You add an inhibitor to your enzyme and you notice that the Vmax has decreased while the Km for enzyme X has increased as a result of adding the inhibitor. What are you able to conclude from this information? The inhibitor must be competitive The amount of total enzyme available to catalyze the reaction in the presence of the inhibitor has likely decreased The enzyme has a higher affinity for its substrate in the presence of the inhibitor The substrate concentration required to reach 1/2 of the maximum velocity for this enzyme has increased as a result of the inhibitor More than one of the above are conclusions that can be drawn from this information
Biochemistry
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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
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