TABLE 3.
Mutant | Sequon | Turnover rate | Relative turnover/fold reduction | Dissociation constant (Kd) |
---|---|---|---|---|
peptide/s | μm | |||
WT | DQNAT | 1.50 ± 0.04 | 1 | 1.02 ± 0.06 |
WT | AQNAT | (3.08 ± 0.13) × 10−5 | 2.05 × 10−5/50,000-fold | –a |
R331A | DQNAT | (3.71 ± 0.08) × 10−3 | 2.47 × 10−3/400-fold | –a |
R331A | AQNAT | (1.03 ± 0.02) × 10−4 | 6.87 × 10−5/15,000-fold | NDb |
a Peptide binding was observed, but no Kd could be determined because the fluorescence anisotropy signal reached only 30–50% saturation at the limiting PglB concentration of 100–150 μm.
b ND, data not determined.