TABLE 2.
Summary of site-directed mutagenesis analysis of the periplasmic domain of OafAa
| Mutant | O:5 signal intensity compared to WT (% ± SEM) | Reason for mutation |
|---|---|---|
| C383,397S (linker) | 107.40 ± 26.80 | Conserved disulfide bonding pairs |
| C439,453S | 185.06 ± 54.63 | Conserved disulfide bonding pairs |
| C567,572S | 49.98 ± 4.33 | Conserved disulfide bonding pairs |
| S437A | 45.59 ± 3.42 | Potential oxyanion hole residue |
| E569A | 99.87 ± 7.01 | Conserved between most C-term Cys pair |
| S412A | 0.36 ± 0.26 | SGNH domain catalytic triad residues |
| D587A | 10.13 ± 1.70 | SGNH domain catalytic triad residues |
| H590A | 0.87 ± 0.62 | SGNH domain catalytic triad residues |
a
Dark gray, point mutants with <1% O:5 signal intensity; light gray, point mutants with <50% O:5 signal intensity. Values represent the average of 2 biological repeats with 3 technical replicates.