(d) The same experiment is performed in the presence of 2 nM inhibitors. The results are: KM = 268µM; Vmax = 49.0μM/sec. Write the Lineweaver-Burk equation for the Enzyme in the presence of an inhibitor. (e) What type of inhibition is described above? Briefly justify your reasoning. (f) What is Kl or Kl' (whichever is relevant) for the inhibitor? (g) Draw v versus [S] for the Adok enzyme in the presence and absence of inhibitor on the plot below (you do not need to be exact and your axes may not be scaled properly, but label | relevant values: KM. KPPM. Vmax, VPPmax. (+1 curve), (-l curve).
(d) The same experiment is performed in the presence of 2 nM inhibitors. The results are: KM = 268µM; Vmax = 49.0μM/sec. Write the Lineweaver-Burk equation for the Enzyme in the presence of an inhibitor. (e) What type of inhibition is described above? Briefly justify your reasoning. (f) What is Kl or Kl' (whichever is relevant) for the inhibitor? (g) Draw v versus [S] for the Adok enzyme in the presence and absence of inhibitor on the plot below (you do not need to be exact and your axes may not be scaled properly, but label | relevant values: KM. KPPM. Vmax, VPPmax. (+1 curve), (-l curve).
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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I need help with parts d-g
a.) For Ado: catalytic efficiency = 4.18 x 106 M-1s-1
For ATP: catalytic efficiency = 12.1 x 107 M-1s-1
b.) Both specificity constants are below the diffusion limit so neither substrate is limiting the reaction rate due to diffusion
c.) Line weaver Burk equation for AdoK enzyme with Ado substrate:
y = 0.68x + (2.04 x 104), where y = 1/vo and x = 1/[Ado]
![(d) The same experiment is performed in the presence of 2 nM inhibitors.
The results are: KM = 268µM; Vmax = 49.0μM/sec. Write the Lineweaver-Burk equation for the
Enzyme in the presence of an inhibitor.
(e) What type of inhibition is described above? Briefly justify your reasoning.
(f) What is Kl or KI' (whichever is relevant) for the inhibitor?
(g) Draw v versus [S] for the Adok enzyme in the presence and absence of inhibitor on the
plot below (you do not need to be exact and your axes may not be scaled properly, but label |
relevant values: KM, KPPM, Vmax, VPP max: (+I curve), (-l curve).](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Ff53216d8-665e-438d-9139-10dafbadcbd3%2Fa4768a52-fd8c-462b-bb7b-a12cb1e5036c%2Fhr6g2h3_processed.png&w=3840&q=75)
Transcribed Image Text:(d) The same experiment is performed in the presence of 2 nM inhibitors.
The results are: KM = 268µM; Vmax = 49.0μM/sec. Write the Lineweaver-Burk equation for the
Enzyme in the presence of an inhibitor.
(e) What type of inhibition is described above? Briefly justify your reasoning.
(f) What is Kl or KI' (whichever is relevant) for the inhibitor?
(g) Draw v versus [S] for the Adok enzyme in the presence and absence of inhibitor on the
plot below (you do not need to be exact and your axes may not be scaled properly, but label |
relevant values: KM, KPPM, Vmax, VPP max: (+I curve), (-l curve).
![The enzyme adenosine kinase (AdoK) is critical for psilocybin biosynthesis. Adok
is a kinase that catalyzes the phosphorylation of adenosine (Ado) to
Adenosine-5'-monophosphate (AMP) using ATP. You obtain the following results of an enzyme
analysis of Adok from the Mushroom P. cubensis:
Total enzyme concentration (M) Substrate KM (M)
Ado
ATP
Ma
35
35
keat (sec ¹)
1.4 x 10³
1.4 x 10³
33.5
11.6
(a) Is the AdoKk enzyme a more efficient enzyme for ATP or Ado substrate? Explain
(b) Does the enzyme approach the diffusion limit for either substrate? Explain
(c) What is the Lineweaver Burk plot equation for the Adok enzyme for the substrate Ado
([S] = [Ado])? (Write the Lineweaver-Burk equation)](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Ff53216d8-665e-438d-9139-10dafbadcbd3%2Fa4768a52-fd8c-462b-bb7b-a12cb1e5036c%2F512yln_processed.png&w=3840&q=75)
Transcribed Image Text:The enzyme adenosine kinase (AdoK) is critical for psilocybin biosynthesis. Adok
is a kinase that catalyzes the phosphorylation of adenosine (Ado) to
Adenosine-5'-monophosphate (AMP) using ATP. You obtain the following results of an enzyme
analysis of Adok from the Mushroom P. cubensis:
Total enzyme concentration (M) Substrate KM (M)
Ado
ATP
Ma
35
35
keat (sec ¹)
1.4 x 10³
1.4 x 10³
33.5
11.6
(a) Is the AdoKk enzyme a more efficient enzyme for ATP or Ado substrate? Explain
(b) Does the enzyme approach the diffusion limit for either substrate? Explain
(c) What is the Lineweaver Burk plot equation for the Adok enzyme for the substrate Ado
([S] = [Ado])? (Write the Lineweaver-Burk equation)
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