Protein Variants | Comment | Organism |
---|---|---|
E274A | site-directed mutagenesis of a residue near the substrate side | Escherichia coli |
E274A | site-directed mutagenesis of an active site residue | Escherichia coli |
M345A | site-directed mutagenesis of an active site residue | Escherichia coli |
N378C | site-directed mutagenesis of a residue near the flavin cofactor side | Escherichia coli |
N378C | site-directed mutagenesis of an active site residue | Escherichia coli |
R226A | site-directed mutagenesis of an active site residue | Escherichia coli |
R342A | site-directed mutagenesis of an active site residue | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
cyclobutadipyrimidine (in DNA) | Escherichia coli | - |
2 pyrimidine residues (in DNA) | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) | cyclic electron-transfer radical mechanism with two fundamental processes, electron-tunneling pathways and cyclobutane ring splitting, the cyclobutane pyrimidine dimer splits in two sequential steps within 90 ps and the electron tunnels between the cofactor and substrate through a remarkable route with an intervening adenine, dynamics and mechanism of cyclobutane pyrimidine dimer repair by DNA photolyase, overview | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
cyclobutadipyrimidine (in DNA) | - |
Escherichia coli | 2 pyrimidine residues (in DNA) | - |
? | |
cyclobutadipyrimidine (in DNA) | various CPD substrates, T-T, T-U, U-T, U-U dimers | Escherichia coli | 2 pyrimidine residues (in DNA) | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CPD photolyase | - |
Escherichia coli |
DNA photolyase | - |
Escherichia coli |
thymine dimer by photolyase | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | absorption spectra of FADH+, FADH radical, and FADH- of wild-type and mutant enzymes, overview. All three flavin species and decays to zero upon completion of repair | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
additional information | electron-tunneling pathways and functional role of adenine moiety of wild-type and mutant enzymes, overview | Escherichia coli |