1). The initial velocity of an enzyme-catalyzed reaction has been determined at several substrate concentrations with and without an inhibitor I. The total enzyme concentration [E]ot present in each experiment is 1.20 x 10 M. [1]-5.00 x10¹ M. (Note: v initial rate or velocity.) [S], M 1.25E-3 2.50E-3 5.00E-3 10.0E-3 v, M/min, no inhibitor 0.480E-3 0.660E-3 0.810E-3 0.920E-3 v, M/min, [1]-5.00x10 M 9.43E-5 1.41E-4 1.70E-4 2.10E-4 a). Use the Lineweaver-Burk plot to determine the values of Vmax and KM at [I] -0.00 mM, and the values of Vmax and KM at 0.500 mM of I. b). What kind of inhibition occurred. c). Calculate the value of K H molecules
1). The initial velocity of an enzyme-catalyzed reaction has been determined at several substrate concentrations with and without an inhibitor I. The total enzyme concentration [E]ot present in each experiment is 1.20 x 10 M. [1]-5.00 x10¹ M. (Note: v initial rate or velocity.) [S], M 1.25E-3 2.50E-3 5.00E-3 10.0E-3 v, M/min, no inhibitor 0.480E-3 0.660E-3 0.810E-3 0.920E-3 v, M/min, [1]-5.00x10 M 9.43E-5 1.41E-4 1.70E-4 2.10E-4 a). Use the Lineweaver-Burk plot to determine the values of Vmax and KM at [I] -0.00 mM, and the values of Vmax and KM at 0.500 mM of I. b). What kind of inhibition occurred. c). Calculate the value of K H molecules
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
Related questions
Question
![1). The initial velocity of an enzyme-catalyzed reaction has been determined at several substrate
concentrations with and without an inhibitor I. The total enzyme concentration [E]ot present in each
experiment is 1.20 x 10 M. [1] = 5.00 x10 M.
(Note: v initial rate or velocity.)
[S], M
1.25E-3
2.50E-3
5.00E-3
10.0E-3
v, M/min, no inhibitor
0.480E-3
0.660E-3
0.810E-3
0.920E-3
v, M/min, 5.00x10 M
9.43E-5
1.41E-4
1.70E-4
2.10E-4
b). What kind of inhibition occurred.
c). Calculate the value of Ki
=
a). Use the Lineweaver-Burk plot to determine the values of Vmax and KM at [1] = 0.00 mM, and the
values of Vmax and KM at 0.500 mM of I.
it in 'How many molecules of](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F3ff92082-cadb-4531-b35c-ccf89a6256de%2F43371c55-2c8d-49e3-a641-d5f63ea2e7fc%2Fg2apken_processed.jpeg&w=3840&q=75)
Transcribed Image Text:1). The initial velocity of an enzyme-catalyzed reaction has been determined at several substrate
concentrations with and without an inhibitor I. The total enzyme concentration [E]ot present in each
experiment is 1.20 x 10 M. [1] = 5.00 x10 M.
(Note: v initial rate or velocity.)
[S], M
1.25E-3
2.50E-3
5.00E-3
10.0E-3
v, M/min, no inhibitor
0.480E-3
0.660E-3
0.810E-3
0.920E-3
v, M/min, 5.00x10 M
9.43E-5
1.41E-4
1.70E-4
2.10E-4
b). What kind of inhibition occurred.
c). Calculate the value of Ki
=
a). Use the Lineweaver-Burk plot to determine the values of Vmax and KM at [1] = 0.00 mM, and the
values of Vmax and KM at 0.500 mM of I.
it in 'How many molecules of
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