Hydrolysis of O-acetyl-ADP-ribose isomers by ADP-ribosylhydrolase 3.

  title={Hydrolysis of O-acetyl-ADP-ribose isomers by ADP-ribosylhydrolase 3.},
  author={Atsushi Kasamatsu and Motoyuki Nakao and Brian Christopher Smith and Lindsay R. Comstock and Tohru Ono and Jiro Kato and John M Denu and Joel Moss},
  journal={The Journal of biological chemistry},
  volume={286 24},
O-acetyl-ADP-ribose (OAADPr), produced by the Sir2-catalyzed NAD(+)-dependent histone/protein deacetylase reaction, regulates diverse biological processes. Interconversion between two OAADPr isomers with acetyl attached to the C-2″ and C-3″ hydroxyl of ADP-ribose (ADPr) is rapid. We reported earlier that ADP-ribosylhydrolase 3 (ARH3), one of three ARH proteins sharing structural similarities, hydrolyzed OAADPr to ADPr and acetate, and poly(ADPr) to ADPr monomers. ARH1 also hydrolyzed OAADPr and… CONTINUE READING
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