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Literature summary extracted from
- Charge redistribution in oxidized and semiquinone E. coli DNA photolyase upon photoexcitation: stark spectroscopy reveals a rationale for the position of Trp382 (2009), J. Am. Chem. Soc., 131, 4795-4807.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.99.3 | Escherichia coli | P00914 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.1.99.3 | - |
Escherichia coli |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 4.1.99.3 | -80°C, 50% glycerol | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.1.99.3 | DNA photolyase | - |
Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.99.3 | FAD | critical W382 residue relative to the flavin for efficient vectorial electron transfer leading to photoreduction | Escherichia coli |  |
| 4.1.99.3 | FADH2 | - |
Escherichia coli | |
| 4.1.99.3 | methenyltetrahydrofolate | - |
Escherichia coli | |
| 4.1.99.3 | additional information | light-driven blue light flavophotoreceptors all operate from the excited state, whether singlet oxidized (e.g., BLUF and LOV domains) or doublet semiquinone | Escherichia coli |
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Release 2023.1 (January 2023)
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