EC 3.2.2.19 - [protein ADP-ribosylarginine] hydrolase

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IntEnz Enzyme Nomenclature
EC 3.2.2.19

Names

Accepted name:
[protein ADP-ribosylarginine] hydrolase
Other names:
Nω-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
ADP-ribose-L-arginine cleavage enzyme
ADP-ribosylarginine hydrolase
ADP-ribose-L-arginine cleaving enzyme
protein-ω-N-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
Systematic name:
protein-Nω-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase

Reactions

Comments:

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

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003875
UniProtKB/Swiss-Prot:

References

  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: 5603-5607 (1985). [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: 10481-10488 (1992). [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: 16736-16740 (1999). [PMID: 10358013]
  4. Takada, T., Iida, K. and Moss, J.
    Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase.
    J. Biol. Chem. 268: 17837-17843 (1993). [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. 231: 115-122 (1996). [PMID: 8678289]

[EC 3.2.2.19 created 1989, modified 2004]