The enzyme β-methylaspartase catalyzes the deamination of β-methylaspartate. For this aspartate reaction in the presence of the inhibitor hydroxymethylaspartate (3.8 M), determine KM and whether the inhibition is competitive or noncompetitive (KI = 1.0 M).
The enzyme β-methylaspartase catalyzes the deamination of β-methylaspartate. For this aspartate reaction in the presence of the inhibitor hydroxymethylaspartate (3.8 M), determine KM and whether the inhibition is competitive or noncompetitive (KI = 1.0 M).
|
[S], M |
V w/o inhibitor, M/s |
V w/ inhibitor, M/s |
|
1x10-4 |
0.0259 |
0.0098 |
|
5x10-4 |
0.0917 |
0.040 |
|
1.5x10-3 |
0.136 |
0.086 |
|
2.5x10-3 |
0.150 |
0.120 |
|
5x10-3 |
0.165 |
0.142 |
In the ABSENCE of inhibitor:
The Lineweaver-Burke equation is 1V=1V= __________ (1[S])(1[S]) + __________, and the KM is __________ M.
In the PRESENCE of inhibitor:
The Lineweaver-Burke equation is 1V=1V= ____________ (1[S])(1[S]) + ___________, and the KM is ___________ M.
The type of inhibition is ____________.
Round-off all answers to two (2) significant figures.
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