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
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
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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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]](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fc94cb5d1-997a-49d0-b0ef-9ec02bf0a187%2F39979c7e-a677-40cc-a183-f4272ceee2a9%2F3d3rzp_processed.png&w=3840&q=75)
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]

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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