Table 2.
Activity of CurM ST variants
| CurM ST variants | % Activitya | Location |
|---|---|---|
| Wild type | 100 | |
| R39A | 1.4 ± 1.1 | PAP binding |
| T43A | 1.1 ± 1.5 | Active site |
| E60A | 0.3 ± 1.0 | Active site |
| E60Q | 0.7 ± 0.6 | Active site |
| H62A | 8 ± 1 | Active site |
| K133A | < 0.1 | Active site |
| S134A | 52 ± 11 | Structural |
| S261A | 131 ± 19 | Flap |
| D266A | 1.9 ± 1.1 | Flap, PAP binding |
| D266N | 3.5 ± 0.9 | Flap, PAP binding |
| P267A | 58 ± 5 | Flap |
| No ST | 0 | |
| No PAPS | 0 | |
a
Raw HPLC chromatogram peak areas for the substrate ((R)-3-hydroxymyristoyl-ACP) and product ((R)-3-sulfomyristoyl-ACP) were used to calculate the fraction of substrate sulfonated. The activity of each variant was normalized to the wild type within each replicate. Mean ± standard deviation from triplicate experiments is shown.