The enzyme ẞ-methylaspartase catalyzes the deamination of ẞ-methylaspartate: CH, NH, OOC-CH-CH-COO CH₁ OOC-CH-CH, COO +NH mesaconate [V. Williams and J. Selbin, J. Biol. Chem. 239, 1636 (1964)] The effects of hydroxymethylaspartate as an inhibitor for this enzyme was studied. The following data wer Substrate Concentration obtained: Reaction Rate without inhibitor (mM) 1 x 10-4 5 x 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 (mM/s) 0.026 0.092 0.136 0.150 0.165 Reaction Rate with inhibitor (mM/s) 0.010 0.040 0.086 0.120 0.142 Use Lineweaver-Burk plot to determine the KM and Vmax of the enzyme in the absence of inhibitor. Moreover, determine as well whether the inhibitor is competitive or noncompetitive. Show the graphs and calculations below.
The enzyme ẞ-methylaspartase catalyzes the deamination of ẞ-methylaspartate: CH, NH, OOC-CH-CH-COO CH₁ OOC-CH-CH, COO +NH mesaconate [V. Williams and J. Selbin, J. Biol. Chem. 239, 1636 (1964)] The effects of hydroxymethylaspartate as an inhibitor for this enzyme was studied. The following data wer Substrate Concentration obtained: Reaction Rate without inhibitor (mM) 1 x 10-4 5 x 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 (mM/s) 0.026 0.092 0.136 0.150 0.165 Reaction Rate with inhibitor (mM/s) 0.010 0.040 0.086 0.120 0.142 Use Lineweaver-Burk plot to determine the KM and Vmax of the enzyme in the absence of inhibitor. Moreover, determine as well whether the inhibitor is competitive or noncompetitive. Show the graphs and calculations below.
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
Can u do only calculation?? And check my graph if correct just Re write my graph and do calculation okk
Transcribed Image Text:9:52
92%
Ans:-
(4)
Y-axis
DUZ
KU
0.16
3.14
KUNDU
Scale
X-axis 1cm 0.5mM
Y-axis = 1cm = 0.62 mm/s
Rean take without inhibito
KUNDUZ
0.12
0.10
0·08
Re tate of with inhibitor
0.06
0 04
0.02
Кт
max
яхах
0.5
1.6
1.5
2.0 2.5 3.0
3.5 4.6
4.5
5.0
substrate conc? (mm)
(do)
☑
![Directions: Solve the following problem:
The enzyme ẞ-methylaspartase catalyzes the deamination of ẞ-methylaspartate:
CH,NH,
CH₁₂
OOC-CH-CH-COOOOC-CH-CH-COO+NH
mesaconate
[V. Williams and J. Selbin, J. Biol. Chem. 239, 1636 (1964)]
The effects of hydroxymethylaspartate as an inhibitor for this enzyme was studied. The following data wer
Substrate Concentration
obtained:
Reaction Rate without
inhibitor
(mM)
1 x 10-4
5 × 10-4
1.5 x 10-3
2.5 x
10-3
5 x 10-3
(mM/s)
0.026
0.092
0.136
0.150
0.165
Reaction Rate with inhibitor
(mM/s)
0.010
0.040
0.086
0.120
0.142
Use Lineweaver-Burk plot to determine the KM and Vmax of the enzyme in the absence of inhibitor.
Moreover, determine as well whether the inhibitor is competitive or noncompetitive. Show the graphs and
calculations below.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fd3cf5230-7915-4462-bd07-8b78c6b9bdec%2Fe8f7d5cf-21f9-4c11-a971-ba3ba15c8c1e%2Fbqi0qep_processed.jpeg&w=3840&q=75)
Transcribed Image Text:Directions: Solve the following problem:
The enzyme ẞ-methylaspartase catalyzes the deamination of ẞ-methylaspartate:
CH,NH,
CH₁₂
OOC-CH-CH-COOOOC-CH-CH-COO+NH
mesaconate
[V. Williams and J. Selbin, J. Biol. Chem. 239, 1636 (1964)]
The effects of hydroxymethylaspartate as an inhibitor for this enzyme was studied. The following data wer
Substrate Concentration
obtained:
Reaction Rate without
inhibitor
(mM)
1 x 10-4
5 × 10-4
1.5 x 10-3
2.5 x
10-3
5 x 10-3
(mM/s)
0.026
0.092
0.136
0.150
0.165
Reaction Rate with inhibitor
(mM/s)
0.010
0.040
0.086
0.120
0.142
Use Lineweaver-Burk plot to determine the KM and Vmax of the enzyme in the absence of inhibitor.
Moreover, determine as well whether the inhibitor is competitive or noncompetitive. Show the graphs and
calculations below.
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