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Literature summary for 4.1.99.3 extracted from
- Enzyme-substrate binding kinetics indicate that photolyase recognizes an extrahelical cyclobutane thymidine dimer (2015), Biochemistry, 54, 6176-6185 .
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | substrate binding and reaction kinetics, fluorescence stopped-flow experiments, overview | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cyclobutadipyrimidine (in DNA) | Escherichia coli | - |
2 pyrimidine residues (in DNA) | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P00914 | strain pMS969 | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cyclobutadipyrimidine (in DNA) | - |
Escherichia coli | 2 pyrimidine residues (in DNA) | - |
? | |
| additional information | direct measurements of photolyase binding to cyclobutane pyrimidine dimers (CPD)-containing undecamer DNA that has been labeled with a fluorophore, photolyase csCPD-DNA binding kinetics detected by fluorescence spectroscopy, overview. Preparation and purification of csCPD-containing oligonucleotides. Photolyase finds its target through a three-dimensional diffusion-controlled search. Photolyase may not recognize an intrahelical CPD but only an extrahelical CPD | Escherichia coli | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DNA photolyase | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | photolyases are structure-specific DNA-repair enzymes that repair DNA lesions that have been induced by ultraviolet (UV) light. Escherichia coli DNA photolyase is a DNA-repair enzyme that repairs cyclobutane pyrimidine dimers (CPDs) which are formed on DNA upon exposure of cells to ultraviolet light. The photolyase catalyzes the CPD monomerization by a light-driven electron-transfer mechanism after the enzyme-substrate complex has formed. The enzyme requires flipping of the CPD site into an extrahelical position. The photolyase is unique in that it requires the two dimerized pyrimidine bases to flip rather than just a single damaged base | Escherichia coli |
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