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Literature summary extracted from
- The missing electrostatic interactions between DNA substrate and Sulfolobus solfataricus DNA photolyase what is the role of charged amino acids in thermophilic DNA binding proteins? (2016), J. Phys. Chem. B, 120, 10234-10242 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.1.99.3 | gene phrB, recombinant expression in Escherichia coli strain Rosetta 2 (DE3) | Saccharolobus solfataricus |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.1.99.3 | additional information | - |
additional information | thermodynamic and kinetic study, overview | Saccharolobus solfataricus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.99.3 | cyclobutadipyrimidine (in DNA) | Saccharolobus solfataricus | - |
2 pyrimidine residues (in DNA) | - |
? |  |
| 4.1.99.3 | cyclobutadipyrimidine (in DNA) | Saccharolobus solfataricus DSM ATCC 35092 / DSM 1617 / JCM 11322 / P2 | - |
2 pyrimidine residues (in DNA) | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.99.3 | Saccharolobus solfataricus | F9VNB1 | i.e. Sulfolobus solfataricus | - |
| 4.1.99.3 | Saccharolobus solfataricus DSM ATCC 35092 / DSM 1617 / JCM 11322 / P2 | F9VNB1 | i.e. Sulfolobus solfataricus | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.1.99.3 | recombinant enzyme from Escherichia coli strain Rosetta 2 (DE3) by desalting gel filtration, Cibacron Blue 3GA affinity and heparin affinity chromatography, and ultrafiltration | Saccharolobus solfataricus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.99.3 | cyclobutadipyrimidine (in DNA) | - |
Saccharolobus solfataricus | 2 pyrimidine residues (in DNA) | - |
? | |
| 4.1.99.3 | cyclobutadipyrimidine (in DNA) | the substrate used in binding experiments, UV-p(dT)10 (denoted as ssDNA), is a single strand oligothymidylate with an average of a single CPD lesion randomly arranged on the 10mer | Saccharolobus solfataricus | 2 pyrimidine residues (in DNA) | - |
? | |
| 4.1.99.3 | cyclobutadipyrimidine (in DNA) | - |
Saccharolobus solfataricus DSM ATCC 35092 / DSM 1617 / JCM 11322 / P2 | 2 pyrimidine residues (in DNA) | - |
? | |
| 4.1.99.3 | cyclobutadipyrimidine (in DNA) | the substrate used in binding experiments, UV-p(dT)10 (denoted as ssDNA), is a single strand oligothymidylate with an average of a single CPD lesion randomly arranged on the 10mer | Saccharolobus solfataricus DSM ATCC 35092 / DSM 1617 / JCM 11322 / P2 | 2 pyrimidine residues (in DNA) | - |
? | |
| 4.1.99.3 | additional information | the first step in the repair mechanism: substrate recognition and binding is s measured by isothermal titration calorimetry | Saccharolobus solfataricus | ? | - |
? | |
| 4.1.99.3 | additional information | the first step in the repair mechanism: substrate recognition and binding is s measured by isothermal titration calorimetry | Saccharolobus solfataricus DSM ATCC 35092 / DSM 1617 / JCM 11322 / P2 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.1.99.3 | DNA photolyase | - |
Saccharolobus solfataricus |
| 4.1.99.3 | PhrB | - |
Saccharolobus solfataricus |
| 4.1.99.3 | SsPL | - |
Saccharolobus solfataricus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.3 | 45 | - |
recombinant enzyme | Saccharolobus solfataricus |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.3 | 25 | 50 | the activity increases slightly from 25-45°C. At 50°C under the solvent conditions of the assay, the SsPL appears to denature after repair of the DNA substrate is mostly complete | Saccharolobus solfataricus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.3 | 7 | - |
assay at | Saccharolobus solfataricus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.99.3 | FAD | enzyme SsPL is an unusual photolyase in that it contains two FAD cofactors. One FAD cofactor is part of the active site of the protein and required for both DNA binding and repair. The second cofactor, the putative accessory chromophore, may play a role as a light-harvesting pigment, it is always present in the fully oxidized FAD state. The active site cycles between FADH-, the fully reduced form required for activity, and FADH radical, the one-electron oxidized or semiquinone form, SsPL is isolated with the active site mainly in the FADH· state. The accessory FAD does not appear to readily undergo any reduction-oxidation chemistry, and it is always found in the fully oxidized state | Saccharolobus solfataricus | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.1.99.3 | additional information | the enzymatic activity and thermodynamics of substrate binding for the enzyme from Sulfolobus solfataricus are directly compared to the enzyme from Escherichia coli, overview. Turnover numbers and catalytic activity are virtually identical, but organic co-solvents may be necessary to maintain activity of the thermophilic protein at higher temperatures. UV-damaged DNA binding to the thermophilic protein is less favorable by about 2 kJ/mol. The enthalpy of binding is about 10 kJ/mol less exothermic for the thermophile, but the amount and type of surface area buried upon DNA binding appears to be somewhat similar. The most important finding is observed when ionic strength studies are used to separate binding interactions into electrostatic and nonelectrostatic contributions, DNA binding to the thermophilic protein appears to lack the electrostatic contributions observed with the mesophilic protein. Reported differences between mesophilic and thermophilic enzymes include an increase in the number of ion pairs/salt bridges, better packing of hydrophobic amino acids, and increased hydrogen bonding for the thermophilic proteins. Comparison of the enthalpy of binding. Analysis of enzyme-substrate interactions, overview | Saccharolobus solfataricus |
| 4.1.99.3 | physiological function | DNA photolyase is a structure-specific DNA repair enzyme that reverses one of the most common types of UV damage in DNA molecules, the cis-syn cyclobutylpyrimidine dimer (CPD) | Saccharolobus solfataricus |
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