b) From the following data on an enzymatic reaction based on competitive inhibition, determine (a) KM for the enzyme, and (b) Kị for the inhibitor-enzyme complex. Substrate Product per hour, Hg Çoncentration, mM No inhibitor 6 mM inhibitor 2.0 139 88 121 149 179 213 313 370 3.0 4.0 10.0 257 15.0 313
b) From the following data on an enzymatic reaction based on competitive inhibition, determine (a) KM for the enzyme, and (b) Kị for the inhibitor-enzyme complex. Substrate Product per hour, Hg Çoncentration, mM No inhibitor 6 mM inhibitor 2.0 139 88 121 149 179 213 313 370 3.0 4.0 10.0 257 15.0 313
Introduction to Chemical Engineering Thermodynamics
8th Edition
ISBN:9781259696527
Author:J.M. Smith Termodinamica en ingenieria quimica, Hendrick C Van Ness, Michael Abbott, Mark Swihart
Publisher:J.M. Smith Termodinamica en ingenieria quimica, Hendrick C Van Ness, Michael Abbott, Mark Swihart
Chapter1: Introduction
Section: Chapter Questions
Problem 1.1P
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Transcribed Image Text:b) From the following data on an enzymatic reaction based on competitive inhibition,
determine (a) KM for the enzyme, and (b) Kị for the inhibitor-enzyme complex.
Substrate
Product per hour, µg
Çoncentration,
mM
No inhibitor
6 mM inhibitor
88
139
179
213
2.0
121
149
3.0
4.0
10.0
313
257
370
313
15.0
![a)
The competitive inhibition model is based on the following premises:
1)
2)
The enzyme lacks absolute specificity
The substrate and the inhibitor compete for active site
E+S+
ES k2, E+P
E+I<,
k_3
EI
3)
Assumptions :
• Based on steady state approximation
d(ES)/ dt = 0=d(EI)/ dt
E+P-ES in negligible
...
• E«S
Constant reactor volume V, temperature (T), and PH
Initial rate (no enzyme degradation)
Derive the Michaelis-Menten equation for competitive inhibition as the following
expression:
V =Vm(S)/{K„[1.0+(I)/K¡]+ S}
where
K = (k_, +k,)k,
V, = k, E,
K; = k_/k,
I=the inhibitor concentration
%3D](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F254ecfd8-ff4e-473b-a995-4fa6e668f57c%2F1dc10317-92a6-4e57-820a-3d925cce022d%2Faey3x2u_processed.jpeg&w=3840&q=75)
Transcribed Image Text:a)
The competitive inhibition model is based on the following premises:
1)
2)
The enzyme lacks absolute specificity
The substrate and the inhibitor compete for active site
E+S+
ES k2, E+P
E+I<,
k_3
EI
3)
Assumptions :
• Based on steady state approximation
d(ES)/ dt = 0=d(EI)/ dt
E+P-ES in negligible
...
• E«S
Constant reactor volume V, temperature (T), and PH
Initial rate (no enzyme degradation)
Derive the Michaelis-Menten equation for competitive inhibition as the following
expression:
V =Vm(S)/{K„[1.0+(I)/K¡]+ S}
where
K = (k_, +k,)k,
V, = k, E,
K; = k_/k,
I=the inhibitor concentration
%3D
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