[S] µM vo(umol ml-'s-1) 320 169 160 132 80.0 92.0 40.0 57.2 20.0 32.6 10.0 17.5
Biochemistry
9th Edition
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
Section: Chapter Questions
Problem 1P
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Question
100%
Initial rate data for an enzyme that obeys Michaelis–Menten kinetics are
shown in the following table. When the enzyme concentration is 3 nmol
ml-1, a Lineweaver–Burk plot of this data gives a line with a y-intercept of
0.00426 (μmol-1 ml s). (a) Calculate kcat for the reaction.
(b) Calculate KM for the enzyme.
(c) When the reactions in part (b) are repeated in the presence of 12 μM of
an uncompetitive inhibitor, the y-intercept of the Lineweaver–Burk plot
is 0.352 (μmol-1 ml s). Calculate K′I for this inhibitor.
![[S] µM vo(umol ml-'s-1)
320
169
160
132
80.0
92.0
40.0
57.2
20.0
32.6
10.0
17.5](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F7c92437c-c247-46c1-a29e-d623448ff740%2Fd6e146a9-65ac-4541-b3c1-7bc4b5d8f49b%2Fn4x6vdn_processed.png&w=3840&q=75)
Transcribed Image Text:[S] µM vo(umol ml-'s-1)
320
169
160
132
80.0
92.0
40.0
57.2
20.0
32.6
10.0
17.5
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