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 × 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.

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
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Directions: Solve the following problem:
The enzyme ẞ-methylaspartase catalyzes the deamination of ẞ-methylaspartate:
CH,NH,
CH
OOC-CH-CH-COOOOC-CH-CH-COO+NH
mesaconate
Williams and Selbin
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 × 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.
Transcribed Image Text:Directions: Solve the following problem: The enzyme ẞ-methylaspartase catalyzes the deamination of ẞ-methylaspartate: CH,NH, CH OOC-CH-CH-COOOOC-CH-CH-COO+NH mesaconate Williams and Selbin 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 × 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.
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