ADP-ribosylhydrolase 1
| ADP-ribosylhydrolase 1 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of human (ADP-ribosyl)hydrolase ARH1 in complex with ADP-ribose (PDB 6G28). | |||||||||
| Identifiers | |||||||||
| EC no. | 3.2.2.19 | ||||||||
| CAS no. | 98668-52-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
(ADP-ribosyl)hydrolase 1, also termed [Protein ADP-ribosylarginine] hydrolase and protein-Nω-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase (EC 3.2.2.19), is an enzyme that in humans is encoded by the ADPRH gene.[1][2][3][4][5] This enzyme is a specific mono(ADP-ribosyl)hydrolase that catalyses the removal of an ADP-ribosyl modification from target arginine residues of protein substrates.[4][6] The chemical reactions can formally be described as follows:
- Nω-(ADP-D-ribosyl)-L-arginyl-[protein] + H2O ADP-D-ribose + L-arginyl-[protein]
- In addition, the enzyme can reverse the ADP-ribosylation of free arginine:[6][7][8]
- Nω-(ADP-D-ribosyl)-L-arginine + H2O ADP-D-ribose + L-arginine
See also
[edit]References
[edit]- ^ Moss J, Jacobson MK, Stanley SJ (September 1985). "Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme". Proceedings of the National Academy of Sciences of the United States of America. 82 (17): 5603–7. doi:10.1073/pnas.82.17.5603. PMC 390599. PMID 2994036.
- ^ Moss J, Stanley SJ, Nightingale MS, Murtagh JJ, Monaco L, Mishima K, Chen HC, Williamson KC, Tsai SC (May 1992). "Molecular and immunological characterization of ADP-ribosylarginine hydrolases". The Journal of Biological Chemistry. 267 (15): 10481–8. doi:10.1016/S0021-9258(19)50043-6. PMID 1375222.
- ^ Konczalik P, Moss J (June 1999). "Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases". The Journal of Biological Chemistry. 274 (24): 16736–40. doi:10.1074/jbc.274.24.16736. PMID 10358013.
- ^ a b Takada T, Iida K, Moss J (August 1993). "Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase". The Journal of Biological Chemistry. 268 (24): 17837–43. doi:10.1016/S0021-9258(17)46780-9. PMID 8349667.
- ^ Ohno T, Tsuchiya M, Osago H, Hara N, Jidoi J, Shimoyama M (October 1995). "Detection of arginine-ADP-ribosylated protein using recombinant ADP-ribosylarginine hydrolase". Analytical Biochemistry. 231 (1): 115–22. doi:10.1006/abio.1995.1510. PMID 8678289.
- ^ a b Rack, Johannes Gregor Matthias; Ariza, Antonio; Drown, Bryon S.; Henfrey, Callum; Bartlett, Edward; Shirai, Tomohiro; Hergenrother, Paul J.; Ahel, Ivan (2018-12-20). "(ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition". Cell Chemical Biology. 25 (12): 1533–1546.e12. doi:10.1016/j.chembiol.2018.11.001. ISSN 2451-9448. PMC 6309922. PMID 30472116.
- ^ Drown, Bryon S.; Shirai, Tomohiro; Rack, Johannes Gregor Matthias; Ahel, Ivan; Hergenrother, Paul J. (2018-12-20). "Monitoring Poly(ADP-ribosyl)glycohydrolase Activity with a Continuous Fluorescent Substrate". Cell Chemical Biology. 25 (12): 1562–1570.e19. doi:10.1016/j.chembiol.2018.09.008. ISSN 2451-9448. PMC 6309520. PMID 30318463.
- ^ Moss, Joel; Oppenheimer, Norman J.; West, Robert E.; Stanley, Sally J. (September 1986). "Amino acid specific ADP-ribosylation: substrate specificity of an ADP-ribosylarginine hydrolase from turkey erythrocytes". Biochemistry. 25 (19): 5408–5414. doi:10.1021/bi00367a010. ISSN 0006-2960. PMID 3778868.
External links
[edit]- (protein+ADP-ribosylarginine)+hydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
