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Literature summary for 4.1.99.13 extracted from
- Spectroscopic characterization of a (6-4) photolyase from the green alga Ostreococcus tauri (2009), J. Photochem. Photobiol. B Biol., 96, 38-48.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Ostreococcus tauri |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Ostreococcus tauri | Q5IFN1 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Ostreococcus tauri |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| OtCPF1 | - |
Ostreococcus tauri |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | non-covalently bound to the enzyme. Flavin to apoprotein molecular ratio of 64%. FAD is present in three different redox states: the fully oxidized form (FADox, 82%), the neutral semiquinone (14%) and the fully reduced anion (4%) | Ostreococcus tauri |  |
| additional information | lacks a light-harvesting chromophore | Ostreococcus tauri |
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Release 2023.1 (January 2023)
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