The steady-state kinetics of an enzyme are studied in the absence and presence of an inhibitor (inhibitor A). The initial rate is given as a function of substrate concentration in the following table:
| v [(mmol/ | L)min−1] |
[S] (mmol/L) | No inhibitor | Inhibitor A |
1.25 | 1.72 | 0.98 |
1.67 | 2.04 | 1.17 |
2.50 | 2.63 | 1.47 |
5.00 | 3.33 | 1.96 |
10.00 | 4.17 | 2.38 |
(a) What kind of inhibition (competitive, uncompetitive, or mixed) is involved?
(b) Determine Vmax and KM in the absence and presence of inhibitor.
We need at least 10 more requests to produce the solution.
0 / 10 have requested this problem solution
The more requests, the faster the answer.