Table 1.
Properties of pLG72 variants (Sacchi et al., 2017).
| pLG72 variants | ||||
|---|---|---|---|---|
| R30 (wild-type) | R30K | K62E | ||
| Binding Kd (μM) | FADa | 54.2 ± 9.3 | 5.07 ± 3.5 | 84.4 ± 3.2 |
| FMNa | 68.9 ± 1.9 | 36.4 ± 3.2 | 50.5 ± 4.5 | |
| CPZa | 1.69 ± 0.09 | 1.56 ± 0.20 | 1.28 ± 0.03 | |
| GDPa | 287 ± 22 | 546 ± 82 | 690 ± 55 | |
| GTPγSa | 72.5 ± 14.9 | 40.0 ± 8.2 | 64.6 ± 14.8 | |
| hDAAOb | 3.30 ± 1.00 | 2.15 ± 0.45 | 3.40 ± 1.07 | |
| (2.7)c (8.3)d | ||||
| hDAAO inhibitione (%) | 53 | 15 | 8 | |
| D-/(D+L)-serinef (%) | 3.09 ± 1.06 | 3.52 ± 1.07 | 3.68 ± 0.97 | |
| Half-life (min) | 23.9 | 13.6 | 21.0 | |
a
Binding was determined following changes in protein fluorescence.
b
Determined from SPR analysis.
c
Sacchi et al. (2008).
d
Birolo et al. (2016).
a−dStandard deviation was calculated from curve fitting.
e
At 1:2 hDAAO:pLG72 ratio and 30 min of incubation.
f
Determined by HPLC analysis; standard deviation arises from measurement replicates.