IPR004808
AP endonuclease 1
InterPro entry
Short name | AP_endonuc_1 |
Overlapping homologous superfamilies | |
family relationships |
Description
AP endonucleases can be classified into two families based on sequence similarity. This family contains members of AP endonuclease family 1. They are endonucleases that remove the damaged DNA at cytosines and guanines by cleaving on the 3'-side of the AP site by a beta-elimination reaction
[1, 2]. The proteins contain glutamate which has been shown
[1] in the Escherichia coli enzyme to bind a divalent metal ion such as magnesium or manganese.
DNA damaging agents such as the anti-tumour drugs bleomycin and neocarzinostatin or those that generate oxygen radicals produce a variety of lesions in DNA. Amongst these is base-loss which forms apurinic/apyrimidinic (AP) sites or strand breaks with atypical 3' termini. DNA repair at the AP sites is initiated by specific endonuclease cleavage of the phosphodiester backbone. Such endonucleases are also generally capable of removing blocking groups from the 3' terminus of DNA strand breaks.
References
1.Structure and function of the multifunctional DNA-repair enzyme exonuclease III. Mol CD, Kuo CF, Thayer MM, Cunningham RP, Tainer JA. Nature 374, 381-6, (1995). View articlePMID: 7885481
GO terms
biological process
molecular function
cellular component
- None
Cross References
Representative structure
1ako: EXONUCLEASE III FROM ESCHERICHIA COLI