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Chemical Compound Review

ADP-Ribose-arg     2-[[5-[[[[5-(6-aminopurin-9- yl)-3,4...

Synonyms: AC1Q5SLK, AR-1D6377, AC1L2Q3T, ADP-Ribosylarginine, Arginine(ADP-ribose)
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Disease relevance of ADP-Ribosylarginine


High impact information on ADP-Ribosylarginine

  • ADP-ribosylarginine hydrolase, which preferentially hydrolyzes the alpha-anomer of ADP-ribosylarginine, released [U-14C]arginine from ADP-ribosyl[U-14C]arginine synthesized by mRT6.1, consistent with the conclusion that mRt6.1 catalyzes a stereospecific Sn2-like reaction [3].
  • 32PO4 attached to GSIII during bacterial growth as part of the modifying group could be removed by treatment with snake venom phosphodiesterase or by turkey erythrocyte ADP-ribosylarginine hydrolase [4].
  • To test the hypothesis that ADP ribosylation of actin may occur with the induction of apoptosis, an in vivo assay of mono-ADPRT activity using an antibody against ADP-ribosylarginine was used [5].
  • Since ADP-ribosylarginine hydrolase, the enzyme responsible for cleavage of the ADP-ribosylarginine bond and a component with the transferase of a putative ADP-ribosylation cycle, is cytosolic, whereas the transferase is attached via a GPI-anchor to the cell surface, the processing of ADP-ribosylated integrin alpha 7 was investigated [6].

Gene context of ADP-Ribosylarginine


  1. Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases. Konczalik, P., Moss, J. J. Biol. Chem. (1999) [Pubmed]
  2. ADP-ribosylarginine glycohydrolase catalyzing the release of ADP-ribose from the cholera toxin-modified alpha-subunits of GTP-binding proteins. Maehama, T., Nishina, H., Katada, T. J. Biochem. (1994) [Pubmed]
  3. Characterization of mouse Rt6.1 NAD:arginine ADP-ribosyltransferase. Moss, J., Stevens, L.A., Cavanaugh, E., Okazaki, I.J., Bortell, R., Kanaitsuka, T., Mordes, J.P., Greiner, D.L., Rossini, A.A. J. Biol. Chem. (1997) [Pubmed]
  4. ADP-ribosylation of Rhizobium meliloti glutamine synthetase III in vivo. Liu, Y., Kahn, M.L. J. Biol. Chem. (1995) [Pubmed]
  5. Inhibition of mono-ADP-ribosyltransferase activity during the execution phase of apoptosis prevents apoptotic body formation. Lodhi, I.J., Clift, R.E., Omann, G.M., Sweeney, J.F., McMahon, K.K., Hinshaw, D.B. Arch. Biochem. Biophys. (2001) [Pubmed]
  6. The alpha 7 integrin as a target protein for cell surface mono-ADP-ribosylation in muscle cells. Zolkiewska, A., Moss, J. Adv. Exp. Med. Biol. (1997) [Pubmed]
  7. Processing of ADP-ribosylated integrin alpha 7 in skeletal muscle myotubes. Zolkiewska, A., Moss, J. J. Biol. Chem. (1995) [Pubmed]
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