EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.99.13 | recombinant protein expressed in Escherichia coli | Drosophila melanogaster |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.1.99.13 | additional information | the predicted amino acid sequence of the human protein has 48% identity with the Drosophila (6-4)photolyase over the entire protein | Homo sapiens |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
4.1.99.13 | 62000 | - |
deduced from cDNA | Drosophila melanogaster |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.99.13 | Drosophila melanogaster | - |
- |
- |
4.1.99.13 | Homo sapiens | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.99.13 | by using affinity chromatography and UV-irradiated DNA attached beads | Drosophila melanogaster |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
4.1.99.13 | (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 | Drosophila melanogaster | |
4.1.99.13 | (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 | Homo sapiens |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
4.1.99.13 | additional information | by Northern blot analysis it is demonstrated that the transcript is expressed in multiple tissues | Homo sapiens | - |
4.1.99.13 | ovary | by Northern blot analysis it is demonstrated that the transcript is expressed at highest level only in adult ovary | Drosophila melanogaster | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.99.13 | (6-4) photoproduct (in DNA) | - |
Drosophila melanogaster | 2 pyrimidine residues (in DNA) | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.99.13 | (6-4) photolyase | - |
Drosophila melanogaster |
4.1.99.13 | human (6-4) photolyase homologous protein | - |
Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.99.13 | FAD | - |
Drosophila melanogaster | |
4.1.99.13 | FAD | - |
Homo sapiens |