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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)

Zolkiewska, A. et al., Moss, J. et al., Zolkiewska, A. et al., Liu, Y. et al., Lodhi, I.J. et al., et al.

Konczalik, Moss,

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Disease relevance of ADP-Ribosylarginine

ADP-ribosylarginine hydrolases from mammalian tissues and Rhodospirillum rubrum exhibit three regions of similarity in deduced amino acid sequence [1].
A rat glycohydrolase which catalyzes the hydrolysis of ADP-ribosylarginine was expressed in Escherichia coli and purified to homogeneity for characterization of its enzymatic properties [2].

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

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, the processing of ADP-ribosylated integrin alpha 7 was investigated [7].

References

Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases. Konczalik, P., Moss, J. J. Biol. Chem. (1999) [Pubmed]
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]
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]
ADP-ribosylation of Rhizobium meliloti glutamine synthetase III in vivo. Liu, Y., Kahn, M.L. J. Biol. Chem. (1995) [Pubmed]
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]
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]
Processing of ADP-ribosylated integrin alpha 7 in skeletal muscle myotubes. Zolkiewska, A., Moss, J. J. Biol. Chem. (1995) [Pubmed]

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