Michaelis-Menten analysis of enzyme kinetics has some limitations about the conditions under which it can be applied. These include all of the following except one-choose the one that is not true. O The kinetics must be analyzed in the early part of the time course (i.e. measuring the initial velocity), before product has accumulated to a significant level. O The concentration of the enzyme-substrate complex is constant. O The concentration of the enzyme-substrate complex (ES) is greater than 50% of total enzyme. The turnover number (kcat) for an enzyme is O the number of times it can catalyze a reaction before it dies. O the maximum number of substrate molecules that the enzyme can bind at one time. O the maximum rate at which the enzyme's active site can catalyze the reaction. O the number of times the enzyme can roll over and play dead before you have to give it a treat.

Chemistry & Chemical Reactivity
10th Edition
ISBN:9781337399074
Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel
Publisher:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel
Chapter14: Chemical Kinetics: The Rates Of Chemical Reactions
Section14.7: Reaction Mechanisms
Problem 1.2ACP
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Michaelis-Menten analysis of enzyme kinetics has some limitations about the conditions under
which it can be applied. These include all of the following except one-choose the one that is not
true.
O The kinetics must be analyzed in the early part of the time course (i.e. measuring the initial velocity), before
product has accumulated to a significant level.
O The concentration of the enzyme-substrate complex is constant.
O The concentration of the enzyme-substrate complex (ES) is greater than 50% of total enzyme.
The turnover number (kcat) for an enzyme is.
O the number of times it can catalyze a reaction before it dies.
O the maximum number of substrate molecules that the enzyme can bind at one time.
O the maximum rate at which the enzyme's active site can catalyze the reaction.
O the number of times the enzyme can roll over and play dead before you have to give it a treat.
An uncompetitive inhibitor.
O binds at the active site at the enzyme, in competition with the substrate.
O always binds at a site far from the active site.
O never mimics a transition state of the reaction.
O would lead to a set of parallel lines from Lineweaver-Burke analysis at different inhibitor concentrations.
Transcribed Image Text:Michaelis-Menten analysis of enzyme kinetics has some limitations about the conditions under which it can be applied. These include all of the following except one-choose the one that is not true. O The kinetics must be analyzed in the early part of the time course (i.e. measuring the initial velocity), before product has accumulated to a significant level. O The concentration of the enzyme-substrate complex is constant. O The concentration of the enzyme-substrate complex (ES) is greater than 50% of total enzyme. The turnover number (kcat) for an enzyme is. O the number of times it can catalyze a reaction before it dies. O the maximum number of substrate molecules that the enzyme can bind at one time. O the maximum rate at which the enzyme's active site can catalyze the reaction. O the number of times the enzyme can roll over and play dead before you have to give it a treat. An uncompetitive inhibitor. O binds at the active site at the enzyme, in competition with the substrate. O always binds at a site far from the active site. O never mimics a transition state of the reaction. O would lead to a set of parallel lines from Lineweaver-Burke analysis at different inhibitor concentrations.
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