• Corpus ID: 25874382

On the recognition and cleavage mechanism of Escherichia coli endodeoxyribonuclease V, a possible DNA repair enzyme.

@article{Demple1982OnTR,
  title={On the recognition and cleavage mechanism of Escherichia coli endodeoxyribonuclease V, a possible DNA repair enzyme.},
  author={Bruce Demple and Stuart Linn},
  journal={The Journal of biological chemistry},
  year={1982},
  volume={257 6},
  pages={
          2848-55
        }
}
  • B. Demple, S. Linn
  • Published 25 March 1982
  • Biology, Chemistry
  • The Journal of biological chemistry
Escherichia coli endodeoxyribonuclease V acts at many sites of damage in duplex DNA, including apurinic/apyrimidinic sites, lesions induced by ultraviolet light which are not pyrimidine dimers, adducts of 7-bromomethylbenz[a]anthracene, and, as demonstrated earlier (Gates, F. T., and Linn, S. (1977a) J. Biol. Chem. 252. 1647-1653), it degrades uracil-containing duplex DNA most efficiently. The cleavage rate increases with increasing substitution of uracil for thymine in T5 DNA, with a… 

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  • Biology, Chemistry
    The Journal of biological chemistry
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Structural basis for incision at deaminated adenines in DNA and RNA by endonuclease V.
Cleavage of deoxyoxanosine-containing oligodeoxyribonucleotides by bacterial endonuclease V.
TLDR
Hypothetic models of oxanine-containing base pairs and deaminated base recognition mechanism are presented and the cleavage of double-stranded oxanosine- containing DNA was approximately 6-fold less efficient than that ofdouble-Stranded inosine-contained DNA.
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Zntroduction to Ultraviolet Photobiology
  • 1967
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