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.
Case Studies In Health Information Management
3rd Edition
ISBN:9781337676908
Author:SCHNERING
Publisher:SCHNERING
Chapter3: Informatics, Analytics, And Data use
Section: Chapter Questions
Problem 3.34.4C
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