Substrate specificity of human endonuclease III (hNTH1). Effect of human APE1 on hNTH1 activity.

@article{Marenstein2003SubstrateSO,
  title={Substrate specificity of human endonuclease III (hNTH1). Effect of human APE1 on hNTH1 activity.},
  author={Dina R Marenstein and Michael K. Chan and Alvin Altamirano and Ashis K Basu and Robert J. Boorstein and Richard P. Cunningham and George W. Teebor},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 11},
  pages={9005-12}
}
Base excision repair of oxidized pyrimidines in human DNA is initiated by the DNA N-glycosylase/apurinic/apyrimidinic (AP) lyase, human NTH1 (hNTH1), the homolog of Escherichia coli endonuclease III (Nth). In contrast to Nth, the DNA N-glycosylase activity of hNTH1 is 7-fold greater than its AP lyase activity when the DNA substrate contains a thymine glycol (Tg) opposite adenine (Tg:A) (Marenstein, D. R., Ocampo, M. T. A., Chan, M. K., Altamirano, A., Basu, A. K., Boorstein, R. J., Cunningham… CONTINUE READING