ADP-ribosylarginine hydrolase
(Protein ADP-ribosylarginine) hydrolase (EC 3.2.2.19, 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.
References
- ↑ Moss, J., Jacobson, M.K. and 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. PMID 2994036.
- ↑ 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. (1992). "Molecular and immunological characterization of ADP-ribosylarginine hydrolases". J. Biol. Chem. 267 (15): 10481–10488. PMID 1375222.
- ↑ Konczalik, P. and 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.
- ↑ Takada, T., Iida, K. and Moss, J. (1993). "Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase". J. Biol. Chem. 268 (24): 17837–17843. PMID 8349667.
- ↑ Ohno, T., Tsuchiya, M., Osago, H., Hara, N., Jidoi, J. and Shimoyama, M. (1995). "Detection of arginine-ADP-ribosylated protein using recombinant ADP-ribosylarginine hydrolase". Anal. Biochem. 10 (1): 115–122. doi:10.1006/abio.1995.1510. PMID 8678289.
External links
|
---|
| Activity | |
---|
| Regulation | |
---|
| Classification | |
---|
| Types | |
---|
|