Activating Compound | Comment | Organism | Structure |
---|---|---|---|
DTT | - |
Xenopus laevis |
Cloned (Comment) | Organism |
---|---|
expressed as a GST-fusion protein in Escherichia coli | Xenopus laevis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Na+ | - |
Xenopus laevis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
T(6-4)T photoproduct (in DNA) | Xenopus laevis | - |
2 thymine residues (in DNA) | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Xenopus laevis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
by using glutathione-sepharose columns | 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 |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
(6-4) photolyase binds to T[6-4]T in double stranded DNA with high affinity (KD= 10*exp-9) and to T[6-4]T in single-stranded DNA with slightly lower-affinity (KD= 2*10 exp-8). Majority of the T[64]T-(6-4) photolyase complex dissociates very slowly (koff= 2.9* 10exp-5/sec). Its absolute action spectrum without a second chromophore in the 350-600 nm region closely matches the absorption spectrum of the enzyme | Xenopus laevis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
T(6-4)T photoproduct (in DNA) | - |
Xenopus laevis | 2 thymine residues (in DNA) | - |
? |
Synonyms | Comment | Organism |
---|---|---|
(6-4) photolyase | - |
Xenopus laevis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Xenopus laevis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Xenopus laevis |