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: Cleaves the [[N-glycosidic bond]] between the 5'-[[pyrimidine]] residue in cyclobutadipyrimidine (in DNA) and the corresponding [[deoxyribose|deoxy-D-ribose]] residue
: Cleaves the [[N-glycosidic bond]] between the 5'-[[pyrimidine]] residue in cyclobutadipyrimidine (in DNA) and the corresponding [[deoxyribose|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 [[DNA AP lyase]] activity against the [[AP site]] produced by this reaction.
The only family of enzymes known to have this activity is represented by a [[phage T4]] protein. This family also has [[DNA-(apurinic or apyrimidinic site) lyase|AP lyase]] activity against the [[AP site]] produced by this reaction.


== References ==
== References ==

Revision as of 09:21, 17 January 2021

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. doi:10.1038/285634a0. PMID 6248789.