Organism | UniProt | Comment | Textmining |
---|---|---|---|
Xenopus laevis | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA) | The overall repair reaction consists of two distinct steps, one of which is light-independent and the other one light-dependent. In the initial light-independent step, a 6-iminium ion is thought to be generated via proton transfer induced by two histidines highly conserved among the (6-4) photolyases.This intermediate spontaneously rearranges to form an oxetane intermediate by intramolecular nucleophilic attack. In the subsequent light-driven reaction, one electron is believed to be transferred from the fully reduced FAD cofactor (FADH-) to the oxetane intermediate thus forming a neutral FADH radical and an anionic oxetane radical, which spontaneously fractures. The excess electron is then back-transferred to the flavin radical restoring the fully reduced flavin cofactor and a pair of pyrimidine bases | Xenopus laevis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(6-4) photoproduct (in DNA) | - |
Xenopus laevis | 2 pyrimidine residues (in DNA) | - |
? | |
Dewar photoproduct | although the affinity of the enzyme for the Dewar photoproduct-containing duplex is similar to that for the (6-4) photoproduct containing substrate a repair rate could not be shown. These results indicate that the (6-4) photolyase binds the DNA containing the Dewar photoproduct and induces a structural change in DNA to some extent, suggesting a difference in the binding mode compared to the (6-4) photoproduct | Xenopus laevis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
(6-4) photolyase | - |
Xenopus laevis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Xenopus laevis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Xenopus laevis |