Deoxyribodipyrimidine endonucleosidase
Identifiers
EC no.3.2.2.17
CAS no.75302-33-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
Pyrimidine dimer DNA glycosylase
Identifiers
SymbolPyr_excise
PfamPF03013
InterProIPR004260
CATH2end
SCOP22end / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
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

  1. 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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