Kinetic mechanism of damage site recognition and uracil flipping by Escherichia coli uracil DNA glycosylase.

@article{Stivers1999KineticMO,
  title={Kinetic mechanism of damage site recognition and uracil flipping by Escherichia coli uracil DNA glycosylase.},
  author={James T Stivers and Krzysztof W. Pankiewicz and Kyoichi A. Watanabe},
  journal={Biochemistry},
  year={1999},
  volume={38 3},
  pages={952-63}
}
The DNA repair enzyme uracil DNA glycosylase (UDG) catalyzes hydrolytic cleavage of the N-glycosidic bond of premutagenic uracil residues in DNA by flipping the uracil base from the DNA helix. The mechanism of base flipping and the role this step plays in site-specific DNA binding and catalysis by enzymes are largely unknown. The thermodynamics and kinetics of DNA binding and uracil flipping by UDG have been studied in the absence of glycosidic bond cleavage using substrate analogues containing… CONTINUE READING

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