The KM of an enzyme is 2.5 mM, In the presence of 2 mM of an inhibitor, the intercept at the (1/[S]) axis changes to (- 0.2 mM-1) while the intercept at the 1/Vmax axis stays the same, this inhibitor cannot be overcome by adding more substrate increases KM but does not change Vmax binds to enzyme-substrate complex ES is a noncompetitive inhibitor

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Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
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Chapter1: Chemical Foundations
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The KM of an enzyme is 2.5 mM, In the presence of 2 mM of an inhibitor, the intercept at the (1/[S]) axis
changes to (- 0.2 mM 1) while the intercept at the 1/Vmax axis stays the same, this inhibitor
cannot be overcome by adding more substrate
increases KM but does not change Vmax
binds to enzyme-substrate complex ES
is a noncompetitive inhibitor
Transcribed Image Text:The KM of an enzyme is 2.5 mM, In the presence of 2 mM of an inhibitor, the intercept at the (1/[S]) axis changes to (- 0.2 mM 1) while the intercept at the 1/Vmax axis stays the same, this inhibitor cannot be overcome by adding more substrate increases KM but does not change Vmax binds to enzyme-substrate complex ES is a noncompetitive inhibitor
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