EC Number   |
Protein Variants |
Reference |
|---|
   1.14.20.14 | G166D |
2.5 A resolution structure of G166D WelO5 in complex with 12-epi-fischerindole U shows that Asp166 coordinates FeII and the substrate location observed in wilde-type enzyme WelO5 is retained in the variant enzyme |
-, 748732 |
| 1.14.20.14 | H259F |
mutant enzyme lacks chlorination activity on 12-epi-fischerindole U |
-, 748728 |
| 1.14.20.14 | more |
a WelO5-variant is constructed by swapping the residues 215-232 of WelO5 from Hapalosiphon welwitschii UTEX B1830 to those of WelO5* of Hapalosiphon welwitschii IC-52-3. The variant displays a noticeably enhanced activity towards 12-epi-hapalindole C. The activity of WelO5-var towards 12-epi-hapalindole C is elevated to a comparable level as the wild type WelO5* from Hapalosiphon welwitschii IC-52-3, while retaining its fidelity towards 12-epi-fischerindole U |
-, 746946 |
| 1.14.20.14 | more |
generation of a pair of chimeric proteins by fusing the N-terminal WelO5 (aa1-145) from Hapalosiphon welwitschii UTEX B 1830 with C-terminal AmbO5 (aa146-290) from Fischerella ambigua to give WelO5AmbO5 and vice versa to give AmbO5WelO5. WelO5AmbO5 is able to convert ambiguine C to ambiguine B, albeit at a lower efficiency comparing with wild-type AmbO5, whereas AmbO5WelO5 shows no measurable activity towards ambiguine C under identical assay conditions. This result implicates the C-terminal residues of AmbO5 may play a role on its broadened substrate scope |
-, 746748 |
