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Literature summary for 4.1.99.13 extracted from
- Combined QM/MM investigation on the light-driven electron-induced repair of the (6-4) thymine dimer catalyzed by DNA photolyase (2013), J. Phys. Chem. B, 117, 10071-10079.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Drosophila melanogaster | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| (6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA) | repair photocycle of (6-4) thymine photoproduct by (6-4) photolyase, which involves light absorption by the 8-HDF cofactor and transfer of the excitation energy to the FADH-. Intermolecular Coulombic decay resulting in an electron transfer from FADH? to the dimer initiating the splitting process, mechanism, detailed overview. The mechanism requires the C5-OH transfer from C5 of the 5' thymine to the C4' of the 3' thymine followed by H transfer to the N3' of the 3' thymine. Of two conserved histidine residues, only His365 is protonated | Drosophila melanogaster |
aSynonyms
| Synonyms | Comment | Organism |
|---|---|---|
| (6-4) photolyase | - |
Drosophila melanogaster |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | quantum mechanical/molecular mechanics simulations using X-ray structure of the enzyme-DNA complex, overview | Drosophila melanogaster |
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