The Enzyme Database

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Accepted name: [protein ADP-ribosylarginine] hydrolase
Reaction: (1) protein-Nω-(ADP-D-ribosyl)-L-arginine + H2O = ADP-D-ribose + protein-L-arginine
(2) Nω-(ADP-D-ribosyl)-L-arginine + H2O = ADP-D-ribose + L-arginine
Glossary: ADP-D-ribose = adenosine 5′-(5-deoxy-D-ribofuranos-5-yl diphosphate)
Other name(s): ADP-ribose-L-arginine cleavage enzyme; ADP-ribosylarginine hydrolase; Nω-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase; protein-ω-N-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
Systematic name: protein-Nω-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
Comments: The enzyme will remove ADP-D-ribose from arginine residues in ADP-ribosylated proteins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 98668-52-1
1.  Moss, J., Jacobson, M.K. and Stanley, S.J. Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme. Proc. Natl. Acad. Sci. USA 82 (1985) 5603–5607. [DOI] [PMID: 2994036]
2.  Moss, J., Stanley, S.J., Nightingale, M.S., Murtagh, J.J., Jr., Monaco, L., Mishima, K., Chen, H.C., Williamson, K.C. and Tsai, S.C. Molecular and immunological characterization of ADP-ribosylarginine hydrolases. J. Biol. Chem. 267 (1992) 10481–10488. [PMID: 1375222]
3.  Konczalik, P. and Moss, J. Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases. J. Biol. Chem. 274 (1999) 16736–16740. [DOI] [PMID: 10358013]
4.  Takada, T., Iida, K. and Moss, J. Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase. J. Biol. Chem. 268 (1993) 17837–17843. [PMID: 8349667]
5.  Ohno, T., Tsuchiya, M., Osago, H., Hara, N., Jidoi, J. and Shimoyama, M. Detection of arginine-ADP-ribosylated protein using recombinant ADP-ribosylarginine hydrolase. Anal. Biochem. 10 (1995) 115–122. [DOI] [PMID: 8678289]
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