Conserved structural chemistry for incision activity in structurally non-homologous apurinic/apyrimidinic endonuclease APE1 and endonuclease IV DNA repair enzymes.

@article{Tsutakawa2013ConservedSC,
  title={Conserved structural chemistry for incision activity in structurally non-homologous apurinic/apyrimidinic endonuclease APE1 and endonuclease IV DNA repair enzymes.},
  author={Susan E. Tsutakawa and David S. Shin and C. De Mol and Tadahide Izumi and Andrew S. Arvai and Anil K. Mantha and Bartosz Szczesny and Ivaylo Ivanov and David J. Hosfield and Buddhadev Maiti and Mike E Pique and Kenneth A. Frankel and Kenichi Hitomi and Richard P. Cunningham and Sankar Mitra and John A. Tainer},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 12},
  pages={8445-55}
}
Non-coding apurinic/apyrimidinic (AP) sites in DNA form spontaneously and as DNA base excision repair intermediates are the most common toxic and mutagenic in vivo DNA lesion. For repair, AP sites must be processed by 5' AP endonucleases in initial stages of base repair. Human APE1 and bacterial Nfo represent the two conserved 5' AP endonuclease families in the biosphere; they both recognize AP sites and incise the phosphodiester backbone 5' to the lesion, yet they lack similar structures and… CONTINUE READING

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