V, (μmol-min-¹) 0.35 1/V₂ 0.3 0.25 0.2 0.15 0.1 0.05 0 0 50 100 150 200 250 300 350 400 450 [S] (nm) The enzyme kinetics data were also used to create a double-reciprocal plot of - versus Vo [S] 12 10 8 6

Biochemistry
9th Edition
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Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
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Q22:

The results of kinetic experiments of an unidentified enzyme were used to create a plot of the initial reaction velocity (Vo) versus
the substrate concentration ([S]).
V, (μmol-min-¹)
0.35
1/₂
0.3
0.25
0.2
0.15
0.1
0.05
0
0
50 100 150 200 250 300 350 400 450
The enzyme kinetics data were also used to create a double-reciprocal plot of
12
10
8
6
[S] (nM)
4
-0.01 -0.005 0 0.005 0.01 0.015 0.02 0.025
1/[S]
Does it appear that the enzyme follows Michaelis-Menten kinetics?
versus
1
[S]
Transcribed Image Text:The results of kinetic experiments of an unidentified enzyme were used to create a plot of the initial reaction velocity (Vo) versus the substrate concentration ([S]). V, (μmol-min-¹) 0.35 1/₂ 0.3 0.25 0.2 0.15 0.1 0.05 0 0 50 100 150 200 250 300 350 400 450 The enzyme kinetics data were also used to create a double-reciprocal plot of 12 10 8 6 [S] (nM) 4 -0.01 -0.005 0 0.005 0.01 0.015 0.02 0.025 1/[S] Does it appear that the enzyme follows Michaelis-Menten kinetics? versus 1 [S]
Does it appear that the enzyme follows Michaelis-Menten kinetics?
yes
Vmax
no
cannot be determined
Now use the double-reciprocal plot to determine the maximum velocity, Vmax, and the Michaelis constant, KM, of the enzyme.
=
KM =
μmol-min
nM
Transcribed Image Text:Does it appear that the enzyme follows Michaelis-Menten kinetics? yes Vmax no cannot be determined Now use the double-reciprocal plot to determine the maximum velocity, Vmax, and the Michaelis constant, KM, of the enzyme. = KM = μmol-min nM
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