† 14.) A reversible inhibitor that is unable to bind to the ES complex A) always binds in the active site D) is always a noncompetitive inhibitor B) may be an uncompetitive inhibitor E) results in a decreased Km pP C) results in an increased VmaxªPP F) results in an unaltered Vmaxapp † 15.) On a Lineweaver-Burk plot, a changing y-intercept upon addition of increasing concentration of inhibitor means C) the slope is increasing F) the Vmax PP is unchanged A) the inhibitor can bind to the free enzyme D) the inhibitor can bind to the ES complex B) the Km PP is decreasing E) the Km PP is unchanged 16.) Vmax represents the rate of reaction for an enzyme-substrate pairing under what conditions? B) when [S] =Km F) for all [S] < Km A) when [S] = ∞ E) for all [S] > Km C) when v < Km G) when [S] = 2 Km D) when v > Km
† 14.) A reversible inhibitor that is unable to bind to the ES complex A) always binds in the active site D) is always a noncompetitive inhibitor B) may be an uncompetitive inhibitor E) results in a decreased Km pP C) results in an increased VmaxªPP F) results in an unaltered Vmaxapp † 15.) On a Lineweaver-Burk plot, a changing y-intercept upon addition of increasing concentration of inhibitor means C) the slope is increasing F) the Vmax PP is unchanged A) the inhibitor can bind to the free enzyme D) the inhibitor can bind to the ES complex B) the Km PP is decreasing E) the Km PP is unchanged 16.) Vmax represents the rate of reaction for an enzyme-substrate pairing under what conditions? B) when [S] =Km F) for all [S] < Km A) when [S] = ∞ E) for all [S] > Km C) when v < Km G) when [S] = 2 Km D) when v > Km
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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![† 14.) A reversible inhibitor that is unable to bind to the ES complex
A) always binds in the active site
D) is always a noncompetitive inhibitor
B) may be an uncompetitive inhibitor
E) results in a decreased Kmapp
C) results in an increased Vmax PP
F) results in an unaltered Vmax pp
† 15.) On a Lineweaver-Burk plot, a changing y-intercept upon addition of increasing concentration of inhibitor means
C) the slope is increasing
F) the Vmax PP is unchanged
A) the inhibitor can bind to the free enzyme
D) the inhibitor can bind to the ES complex
B) the KmaPP is decreasing
E) the Km PP is unchanged
app
16.) Vn
represents the rate of reaction for an enzyme-substrate pairing under what conditions?
A) when [S] = ∞
E) for all [S]> Km
max
B) when [S] = Km
F) for all [S] <Km
C) when v < Km
G) when [S] =2 Km
D) when v > Km](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F827d120e-bf38-4d44-bff9-9b992a66941a%2F1e1062a9-54eb-49c2-8be4-b436587ecfc2%2F9xst679_processed.png&w=3840&q=75)
Transcribed Image Text:† 14.) A reversible inhibitor that is unable to bind to the ES complex
A) always binds in the active site
D) is always a noncompetitive inhibitor
B) may be an uncompetitive inhibitor
E) results in a decreased Kmapp
C) results in an increased Vmax PP
F) results in an unaltered Vmax pp
† 15.) On a Lineweaver-Burk plot, a changing y-intercept upon addition of increasing concentration of inhibitor means
C) the slope is increasing
F) the Vmax PP is unchanged
A) the inhibitor can bind to the free enzyme
D) the inhibitor can bind to the ES complex
B) the KmaPP is decreasing
E) the Km PP is unchanged
app
16.) Vn
represents the rate of reaction for an enzyme-substrate pairing under what conditions?
A) when [S] = ∞
E) for all [S]> Km
max
B) when [S] = Km
F) for all [S] <Km
C) when v < Km
G) when [S] =2 Km
D) when v > Km
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