| Deoxyribodipyrimidine endonucleosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.2.17 | ||||||||
| CAS no. | 75302-33-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
| Pyrimidine dimer DNA glycosylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Pyr_excise | ||||||||
| Pfam | PF03013 | ||||||||
| InterPro | IPR004260 | ||||||||
| CATH | 2end | ||||||||
| SCOP2 | 2end / SCOPe / SUPFAM | ||||||||
| |||||||||
| This is the only protein family known, as of January 2021, to confer this activity. | |||||||||
Deoxyribodipyrimidine endonucleosidase (EC 3.2.2.17, pyrimidine dimer DNA-glycosylase, endonuclease V, deoxyribonucleate pyrimidine dimer glycosidase, pyrimidine dimer DNA glycosylase, T4-induced UV endonuclease, PD-DNA glycosylase) is an enzyme with systematic name deoxy-D-ribocyclobutadipyrimidine polynucleotidodeoxyribohydrolase.[1] This enzyme catalyses the following chemical reaction
- Cleaves the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue
The only family of enzymes known to have this activity is represented by a phage T4 protein. This family also has AP lyase activity against the AP site produced by this reaction.
References
- ↑ Haseltine WA, Gordon LK, Lindan CP, Grafstrom RH, Shaper NL, Grossman L (June 1980). "Cleavage of pyrimidine dimers in specific DNA sequences by a pyrimidine dimer DNA-glycosylase of M. luteus". Nature. 285 (5767): 634–41. Bibcode:1980Natur.285..634H. doi:10.1038/285634a0. PMID 6248789. S2CID 2811671.
External links
- Deoxyribodipyrimidine+endonucleosidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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