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.
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