Any feedback?
Literature summary for 4.1.99.3 extracted from
- Spectroscopic and Thermodynamic Comparisons of Escherichia coli DNA Photolyase and Vibrio cholerae Cryptochrome 1 (2010), J. Phys. Chem. B, 114, 7121-7130.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| FAD | FAD binding pocket is similar to that of cryptochrome 1 | Escherichia coli |  |
| FAD | FAD binding pocket is similar to that of photolyase | Vibrio cholerae serotype O1 | |
| FADH2 | FADH-/FADH reduction potential of the cryptochrome 1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding | Vibrio cholerae serotype O1 | |
| FADH2 | FADH-/FADH reduction potential of the cryptochrome1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding | Escherichia coli | |
| additional information | reduction potential is unchanged in the presence of 120× molar excess of Mg-ATP | Escherichia coli | |
| additional information | reduction potential is unchanged in the presence of 120× molar excess of Mg-ATP | Vibrio cholerae serotype O1 |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed from Escherichia coli strain UNC523F transfected with the pUNC2002 plasmid | Vibrio cholerae serotype O1 |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Vibrio cholerae serotype O1 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| isolated with a maltose binding domain, purified by ammonium sulfate precipitation and gel filtration | Vibrio cholerae serotype O1 |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -80°C | Vibrio cholerae serotype O1 |
| -80°C, for years | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cyclobutadipyrimidine in DNA | photolyase binds tighter to substrate than cryptochrome 1, binding constant is slightly sensitive to oxidation state | Escherichia coli | ? | - |
? | |
| cyclobutadipyrimidine in DNA | photolyase binds tighter to substrate than cryptochrome 1, binding constant is slightly sensitive to oxidation state | Vibrio cholerae serotype O1 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Cry-DASH | - |
Vibrio cholerae serotype O1 |
| Cry1 | - |
Vibrio cholerae serotype O1 |
| cryptochrome 1 | - |
Vibrio cholerae serotype O1 |
| DNA photolyase | - |
Escherichia coli |
| photolyase | - |
Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.073 | - |
cyclobutadipyrimidine in DNA | for dsDNA | Escherichia coli | |
| 0.13 | - |
cyclobutadipyrimidine in DNA | for dsDNA | Vibrio cholerae serotype O1 | |
| 0.2167 | - |
cyclobutadipyrimidine in DNA | for ssDNA | Escherichia coli | |
| 0.23 | - |
cyclobutadipyrimidine in DNA | for ssDNA | Vibrio cholerae serotype O1 | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
