Table 1.
TTNs and Kd values of unnatural substrates with PikCD50N and PikCD50NH238A mutants.
substrate | TTN (D50N) | TTN (D50NH238A) | Kd (D50N) μM | Kd (D50NH238A) μM |
---|---|---|---|---|
1 | 896 ± 0.71 | 842 ± 16 | 19 | ND |
8a | 260 ± 11 | 572 ± 18 | 118 ± 21 | 11 ± 0.56 |
8b | 544 ± 23 | 870 ± 38 | 81 ± 15 | 161 ± 25 |
10 | 452 ± 5.0 | 853 ± 38 | 123 ± 14 | 168 ± 19 |
12a | 456 ± 5.0 | 542 ± 30 | 47 ± 3.0 | 19 ± 1.3 |
12b | 485 ± 21 | 538 ± 20 | 28 ± 5.4 | 21 ± 0.70 |
14 | 152 ± 11 | 491 ± 26 | ND | ND |
16a | 602 ± 3.5 | 816 ± 33 | ND | ND |
16b | 580 ± 11 | 922 ± 35 | ND | ND |
The measurement of Kd values for the benzylic amine substrates was inhibited by the background absorbance of these compounds, thus, binding constants were not obtained for 14, 16a, 16b.