Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain.

@article{Patel2005IdentificationOT,
  title={Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain.},
  author={Chandra N. Patel and David W. Koh and Myron K. Jacobson and Marcos Andr{\'e} Matos Oliveira},
  journal={The Biochemical journal},
  year={2005},
  volume={388 Pt 2},
  pages={493-500}
}
PARG [poly(ADP-ribose) glycohydrolase] catalyses the hydrolysis of alpha(1''-->2') or alpha(1'''-->2'') O-glycosidic linkages of ADP-ribose polymers to produce free ADP-ribose. We investigated possible mechanistic similarities between PARG and glycosidases, which also cleave O-glycosidic linkages. Glycosidases typically utilize two acidic residues for catalysis, thus we targeted acidic residues within a conserved region of bovine PARG that has been shown to contain an inhibitor-binding site… CONTINUE READING

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