A novel uracil-DNA glycosylase with broad substrate specificity and an unusual active site.

@article{Sartori2002ANU,
  title={A novel uracil-DNA glycosylase with broad substrate specificity and an unusual active site.},
  author={Alessandro A Sartori and Sorel T Fitz-Gibbon and Hanjing Yang and J. H. Miller and Josef Jiricny},
  journal={The EMBO journal},
  year={2002},
  volume={21 12},
  pages={3182-91}
}
Uracil-DNA glycosylases (UDGs) catalyse the removal of uracil by flipping it out of the double helix into their binding pockets, where the glycosidic bond is hydrolysed by a water molecule activated by a polar amino acid. Interestingly, the four known UDG families differ in their active site make-up. The activating residues in UNG and SMUG enzymes are aspartates, thermostable UDGs resemble UNG-type enzymes, but carry glutamate rather than aspartate residues in their active sites, and the less… CONTINUE READING