ID: | 3.2.2.19 |
---|---|
Description: | [Protein ADP-ribosylarginine] hydrolase. |
Alternative Name: |
N(omega)-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase. ADP-ribosylarginine hydrolase. ADP-ribose-L-arginine cleaving enzyme. ADP-ribose-L-arginine cleavage enzyme. |
Cath: | 1.10.4080.10; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 3.2.2.19 |
BRENDA Enzyme Link: | BRENDA 3.2.2.19 |
KEGG Enzyme Link: | KEGG3.2.2.19 |
BioCyc Enzyme Link: | BioCyc 3.2.2.19 |
ExPASy Enzyme Link: | ExPASy3.2.2.19 |
EC2PDB Enzyme Link: | EC2PDB 3.2.2.19 |
ExplorEnz Enzyme Link: | ExplorEnz 3.2.2.19 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.2.2.19 |
IntEnz Enzyme Link: | IntEnz 3.2.2.19 |
MEDLINE Enzyme Link: | MEDLINE 3.2.2.19 |
RHEA:20784 | H2O + N(omega)-(ADP-D-ribosyl)-L-arginine = ADP-D-ribose + L-arginine |
RULE(radius=1) | [*:1]-[NH;+0:2]-[CH;+0:3](-[*:4])-[*:5].[OH2;+0:6]>>[*:4]-[CH;+0:3](-[*:5])-[OH;+0:6].[*:1]-[NH2;+0:2] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Detection of arginine-ADP-ribosylated protein using recombinant ADP-ribosylarginine hydrolase. | Ohno T, Tsuchiya M, Osago H, Hara N, Jidoi J, Shimoyama M | 1995 Oct 10 | 8678289 |
Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase. | Takada T, Iida K, Moss J | 1993 Aug 25 | 8349667 |
Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme. | Moss J, Jacobson MK, Stanley SJ | 1985 Sep | 2994036 |
Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases. | Konczalik P, Moss J | 1999 Jun 11 | 10358013 |
RHEA:14885 | H2O + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] = ADP-D-ribose + L-arginyl-[protein] |
RULE(radius=1) | [*:1]-[NH;+0:2]-[CH;+0:3](-[*:4])-[*:5].[OH2;+0:6]>>[*:4]-[CH;+0:3](-[*:5])-[OH;+0:6].[*:1]-[NH2;+0:2] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Detection of arginine-ADP-ribosylated protein using recombinant ADP-ribosylarginine hydrolase. | Ohno T, Tsuchiya M, Osago H, Hara N, Jidoi J, Shimoyama M | 1995 Oct 10 | 8678289 |
Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase. | Takada T, Iida K, Moss J | 1993 Aug 25 | 8349667 |
Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme. | Moss J, Jacobson MK, Stanley SJ | 1985 Sep | 2994036 |
Molecular and immunological characterization of ADP-ribosylarginine hydrolases. | Moss J, Stanley SJ, Nightingale MS, Murtagh JJ Jr, Monaco L, Mishima K, Chen HC, Williamson KC, Tsai SC | 1992 May 25 | 1375222 |
Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases. | Konczalik P, Moss J | 1999 Jun 11 | 10358013 |