Mammalian ADP-ribosyltransferases and ADP-ribosylhydrolases

Front Biosci. 2008 May 1;13:6716-29. doi: 10.2741/3184.


ADP-ribosyltransferases (ARTs) and ADP-ribosylhydrolases (ARHs) catalyze opposing reactions, which are termed ADP-ribosylation and de-ADP-ribosylation. ARTs transfer the ADP-ribose unit from NAD (nicotinamide adenine dinucleotide) onto an acceptor, while ARHs release the ADP-ribose from the target. Like protein phosphorylation, ADP-ribosylation is a posttranslational modification regulating protein function. In many cases, ADP-ribosylation inactivates the target protein. Numerous bacterial toxins intoxicate cells by attaching an ADP-ribose moiety to a functionally important amino acid residue, thereby blocking the interaction of the target protein with other proteins. In other cases, ADP-ribosylation activates protein function. On the surface of T cells, ART2.2 ADP-ribosylates the P2X7 purinoceptor on arginine 125, thereby gating the P2X7 ion channel by presenting a ligand to its nucleotide-binding site. ADP-ribosylation is not limited to protein targets and ARTs have been described that ADP-ribosylate DNA, RNA, and small molecules. Mammalian cells express distinct families of ARTs and ARHs. Recently, molecular cloning, site directed mutagenesis and three-dimensional structural analyses of prototype mammalian ARTs and ARHs have shed fresh insight into the structure and function of these intriguing enzymes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • ADP Ribose Transferases / drug effects
  • ADP Ribose Transferases / metabolism*
  • Adenosine Diphosphate / metabolism
  • Animals
  • Bacterial Physiological Phenomena
  • Diphtheria Toxin / toxicity
  • Humans
  • Mammals
  • N-Glycosyl Hydrolases / drug effects
  • N-Glycosyl Hydrolases / metabolism*
  • Nitrogen Fixation


  • Diphtheria Toxin
  • Adenosine Diphosphate
  • ADP Ribose Transferases
  • N-Glycosyl Hydrolases