ADP-ribosylarginine hydrolase

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(Protein ADP-ribosylarginine) hydrolase
EC number
CAS number 98668-52-1
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

(Protein ADP-ribosylarginine) hydrolase (EC, ADP-ribose-L-arginine cleavage enzyme, Nomega-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase, protein-omega-N-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase) is an enzyme with systematic name protein-Nomega-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

(1) protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O ADP-ribose + protein-L-arginine
(2) Nomega-(ADP-D-ribosyl)-L-arginine + H2O ADP-ribose + L-arginine

The enzyme will remove ADP-ribose from arginine residues in ADP-ribosylated proteins.

See also[edit]


  1. ^ Moss, J.; Jacobson, M.K.; Stanley, S.J. (1985). "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 (17): 5603–5607. doi:10.1073/pnas.82.17.5603. PMC 390599Freely accessible. 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.; Tsai, S.C. (1992). "Molecular and immunological characterization of ADP-ribosylarginine hydrolases". J. Biol. Chem. 267 (15): 10481–10488. PMID 1375222. 
  3. ^ Konczalik, P.; Moss, J. (1999). "Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases". J. Biol. Chem. 274 (24): 16736–16740. doi:10.1074/jbc.274.24.16736. PMID 10358013. 
  4. ^ Takada, T.; Iida, K.; Moss, J. (1993). "Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase". J. Biol. Chem. 268 (24): 17837–17843. PMID 8349667. 
  5. ^ Ohno, T.; Tsuchiya, M.; Osago, H.; Hara, N.; Jidoi, J.; Shimoyama, M. (1995). "Detection of arginine-ADP-ribosylated protein using recombinant ADP-ribosylarginine hydrolase". Anal. Biochem. 231 (1): 115–122. doi:10.1006/abio.1995.1510. PMID 8678289. 

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