Activating Compound | Comment | Organism | Structure |
---|---|---|---|
DTT | - |
Xenopus laevis | |
DTT | - |
Crotalus atrox |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Na+ | - |
Xenopus laevis | |
Na+ | - |
Crotalus atrox |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Crotalus atrox | - |
- |
- |
Xenopus laevis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
(6-4) photoproduct DNA photolyase activity is detected in Crotalus atrox fibroblast. Activity is considerably enhanced when a UV-damaged DNA affinity column is used for purification. However, the activity is unstable and it is lost during purification or upon storage at -20° or -70°C for 2-3 months | Crotalus atrox |
protein is isolated from whole cell extracts from Xenopus laevis, purified by using a sepharose column and a UV-damaged DNA affinity column | 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 | |
(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 | Crotalus atrox |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
fibroblast | - |
Crotalus atrox | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
activity is unstable | Crotalus atrox |
Storage Stability | Organism |
---|---|
activity is unstable and it is lost upon storage at -20° or -70°C for 2-3 months | Crotalus atrox |
protein in aliquots is kept at -20°C until further use or stored at -80°C. The protein sample remained active after 6 months storage | Xenopus laevis |
Synonyms | Comment | Organism |
---|---|---|
(6-4) photolyase | - |
Xenopus laevis |
(6-4) photolyase | - |
Crotalus atrox |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Xenopus laevis |
7.4 | - |
assay at | Crotalus atrox |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Xenopus laevis | |
FAD | - |
Crotalus atrox |