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 KmªP C) results in an increased VmaxªPP F) results in an unaltered Vmax*pP www

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 KmªP C) results in an increased VmaxªPP F) results in an unaltered Vmax*pP www

Chemistry for Today: General, Organic, and Biochemistry

9th Edition

ISBN:9781305960060

Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Publisher:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Chapter20: Enzymes

Section: Chapter Questions

Problem 20.51E

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question 14

† 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 VmaxªPP

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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
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