Deoxyribodipyrimidine endonucleosidase |
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Identifiers |
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EC no. | 3.2.2.17 |
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CAS no. | 75302-33-9 |
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Databases |
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IntEnz | IntEnz view |
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BRENDA | BRENDA entry |
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ExPASy | NiceZyme view |
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KEGG | KEGG entry |
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MetaCyc | metabolic pathway |
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PRIAM | profile |
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PDB structures | RCSB PDB PDBe PDBsum |
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Search |
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PMC | articles |
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PubMed | articles |
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NCBI | proteins |
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Pyrimidine dimer DNA glycosylase |
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Identifiers |
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Symbol | Pyr_excise |
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Pfam | PF03013 |
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InterPro | IPR004260 |
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CATH | 2end |
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SCOP2 | 2end / SCOPe / SUPFAM |
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Available protein structures: |
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Pfam | structures / ECOD |
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PDB | RCSB PDB; PDBe; PDBj |
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PDBsum | structure summary |
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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
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Portal:- Biology
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