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Literature summary for 4.1.99.3 extracted from
- Theoretical study of excitation energy transfer in DNA photolyase (2008), J. Phys. Chem. B, 112, 8724-8729.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Synechococcus elongatus PCC 7942 = FACHB-805 | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cyclobutadipyrimidine in DNA | catalyzes photorepair of thymine dimers on UV damaged DNA | Synechococcus elongatus PCC 7942 = FACHB-805 | pyrimidine residues in DNA | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DNA photolyase | - |
Synechococcus elongatus PCC 7942 = FACHB-805 |
| photolyase | - |
Synechococcus elongatus PCC 7942 = FACHB-805 |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| 7,8-didemethyl-8-hydroxy-5-deazariboflavin | - |
Synechococcus elongatus PCC 7942 = FACHB-805 | |
| FADH2 | the photoactivation of FADH- immediately preceding the electron transfer is a key step in the repair mechanism | Synechococcus elongatus PCC 7942 = FACHB-805 | |
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Release 2023.1 (January 2023)
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