NMR determination of lysine pKa values in the Pol lambda lyase domain: mechanistic implications.

@article{Gao2006NMRDO,
  title={NMR determination of lysine pKa values in the Pol lambda lyase domain: mechanistic implications.},
  author={Guanghua Gao and Eugene F. DeRose and Thomas W Kirby and Robert E. London},
  journal={Biochemistry},
  year={2006},
  volume={45 6},
  pages={1785-94}
}
The base excision repair (BER) process requires removal of an abasic deoxyribose-5-phosphate group, a catalytic activity that has been demonstrated for the N-terminal 8 kDa domain of DNA polymerase beta (Pol beta), and for the homologous domain of DNA polymerase lambda (Pol lambda). Previous studies have demonstrated that this activity results from formation of a Schiff base adduct of the abasic deoxyribose C-1' with a lysine residue (K312 in the case of Pol lambda), followed by a beta… CONTINUE READING