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Literature summary for 4.1.99.3 extracted from
- A cryptochrome/photolyase class of enzymes with single-stranded DNA-specific photolyase activity (2006), Proc. Natl. Acad. Sci. USA, 103, 17696-17700.
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | a new class of photolyases with specificity for cyclobutane pyrimidine dimers in ssDNA is defined. Members of these branch are found in bacteria, plants, and animals, and are designated Cry-DASH, because of the lack of significant photorepair activity on dsDNA | Arabidopsis thaliana |
| biotechnology | a new class of photolyases with specificity for cyclobutane pyrimidine dimers in ssDNA is defined. Members of these branch are found in bacteria, plants, and animals, and are designated Cry-DASH, because of the lack of significant photorepair activity on dsDNA | Xenopus laevis |
| biotechnology | a new class of photolyases with specificity for cyclobutane pyrimidine dimers in ssDNA is defined. Members of these branch are found in bacteria, plants, and animals, and are designated Cry-DASH, because of the lack of significant photorepair activity on dsDNA | Vibrio cholerae serotype O1 |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| AtCry1 belonging to the cryptochrome/photolyase class of enzymes called Cry-DASH proteins is shown to possess no photorepair activity under any condition | Arabidopsis thaliana |
| AtCry3 belonging to the cryptochrome/photolyase class of enzymes called Cry-DASH proteins is shown to be photolyases with high degree of specificity for cyclobutane pyrimidine dimers in ssDNA | Arabidopsis thaliana |
| BsUvrC belonging to the cryptochrome/photolyase class of enzymes called Cry-DASH proteins is shown to possess no photorepair activity under any condition | Bacillus subtilis |
| VcCry1 belonging to the cryptochrome/photolyase class of enzymes called Cry-DASH proteins is shown to be photolyases with high degree of specificity for cyclobutane pyrimidine dimers in ssDNA | Vibrio cholerae serotype O1 |
| XlCry-DASH belonging to the cryptochrome/photolyase class of enzymes called Cry-DASH proteins is shown to be photolyases with high degree of specificity for cyclobutane pyrimidine dimers in ssDNA | Xenopus laevis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | - |
- |
- |
| Bacillus subtilis | - |
- |
- |
| Vibrio cholerae serotype O1 | - |
- |
- |
| Xenopus laevis | - |
- |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
AtCry1 shows no photorepair activity under any condition | Arabidopsis thaliana |
| additional information | - |
BsUvrC shows no photorepair activity under any condition | Bacillus subtilis |
| additional information | - |
it is shown by in vitro and in vivo by photoreactivation assays and electrophoretic mobility shift assays that AtCry3, as a member of the Cry-DASH enzymes, is specific for cyclobutane pyrimidine dimers in ssDNA | Arabidopsis thaliana |
| additional information | - |
it is shown by in vitro and in vivo by photoreactivation assays and electrophoretic mobility shift assays that VcCry1, as a member of the Cry-DASH enzymes,is specific for cyclobutane pyrimidine dimers in ssDNA | Vibrio cholerae serotype O1 |
| additional information | - |
it is shown by in vitro and in vivo by photoreactivation assays and electrophoretic mobility shift assays that XlCry-DASH, as a member of the Cry-DASH enzymes, is specific for cyclobutane pyrimidine dimers in ssDNA | Xenopus laevis |
| additional information | - |
it is shown that VcCry1 repairs photodimers in the deoxyribonucleotide homopolymers poly dU (uracil cyclobutane dimer) and poly dT much more efficiently than the dimers in the ribopolynucleotide homopolymer | Vibrio cholerae serotype O1 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cyclobutadipyrimidine in DNA | AtCry3 repairs the dimer but only in ssDNA | Arabidopsis thaliana | 2 pyrimidine residues in DNA | - |
? |  |
| cyclobutadipyrimidine in DNA | VcCry1 repairs the dimer but only in ssDNA | Vibrio cholerae serotype O1 | 2 pyrimidine residues in DNA | - |
? | |
| cyclobutadipyrimidine in DNA | XlCry-DASH repairs the dimer but only in ssDNA | Xenopus laevis | 2 pyrimidine residues in DNA | - |
? | |
| cyclobutadipyrimidine in RNA | - |
Arabidopsis thaliana | 2 pyrimidine residues in RNA | - |
? | |
| cyclobutadipyrimidine in RNA | - |
Xenopus laevis | 2 pyrimidine residues in RNA | - |
? | |
| cyclobutadipyrimidine in RNA | - |
Vibrio cholerae serotype O1 | 2 pyrimidine residues in RNA | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AtCry1 | - |
Arabidopsis thaliana |
| AtCry3 | - |
Arabidopsis thaliana |
| BsUvrC | - |
Bacillus subtilis |
| Cry-DASH | - |
Bacillus subtilis |
| Cry-DASH | - |
Arabidopsis thaliana |
| Cry-DASH | - |
Xenopus laevis |
| Cry-DASH | - |
Vibrio cholerae serotype O1 |
| VcCry1 | - |
Vibrio cholerae serotype O1 |
| XlCry-DASH | - |
Xenopus laevis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Arabidopsis thaliana |
| 7.5 | - |
assay at | Xenopus laevis |
| 7.5 | - |
assay at | Vibrio cholerae serotype O1 |
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