1.14.20.14: hapalindole-type alkaloid chlorinase
This is an abbreviated version!
For detailed information about hapalindole-type alkaloid chlorinase, go to the full flat file.
Word Map on EC 1.14.20.14
-
1.14.20.14
-
halogenase
-
chlorination
-
unactivated
-
late-stage
-
non-heme
-
welwitindolinone
-
biocatalyst
-
structure-guided
-
2-oxo-glutarate
-
medicine
- 1.14.20.14
- halogenase
-
chlorination
-
unactivated
-
late-stage
-
non-heme
-
welwitindolinone
-
biocatalyst
-
structure-guided
- 2-oxo-glutarate
- medicine
Reaction
Synonyms
ambO5, AmbO5 protein, welO5, WelO5 protein, WelO5*
ECTree
Advanced search results
Engineering
Engineering on EC 1.14.20.14 - hapalindole-type alkaloid chlorinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
H259F
mutant enzyme lacks chlorination activity on 12-epi-fischerindole U
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
-
H259F
-
mutant enzyme lacks chlorination activity on 12-epi-fischerindole U
-
additional information
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
additional information
-
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
additional information
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
additional information
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
additional information
-
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
-
additional information
-
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
-
additional information
-
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
-