Biology:ADP-ribosylarginine hydrolase
From HandWiki
| (Protein ADP-ribosylarginine) hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of human (ADP-ribosyl)hydrolase ARH1 in complex with ADP-ribose (PDB 6G28). | |||||||||
| Identifiers | |||||||||
| EC number | 3.2.2.19 | ||||||||
| CAS number | 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 | ||||||||
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(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 [math]\displaystyle{ \rightleftharpoons }[/math] 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 [math]\displaystyle{ \rightleftharpoons }[/math] ADP-D-ribose + L-arginine
See also
References
- ↑ "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. September 1985. doi:10.1073/pnas.82.17.5603. PMID 2994036.
- ↑ "Molecular and immunological characterization of ADP-ribosylarginine hydrolases". The Journal of Biological Chemistry 267 (15): 10481–8. May 1992. doi:10.1016/S0021-9258(19)50043-6. PMID 1375222.
- ↑ "Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases". The Journal of Biological Chemistry 274 (24): 16736–40. June 1999. doi:10.1074/jbc.274.24.16736. PMID 10358013.
- ↑ 4.0 4.1 "Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase". The Journal of Biological Chemistry 268 (24): 17837–43. August 1993. doi:10.1016/S0021-9258(17)46780-9. PMID 8349667.
- ↑ "Detection of arginine-ADP-ribosylated protein using recombinant ADP-ribosylarginine hydrolase". Analytical Biochemistry 231 (1): 115–22. October 1995. doi:10.1006/abio.1995.1510. PMID 8678289.
- ↑ 6.0 6.1 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. PMID 30472116. PMC 6309922. https://pubmed.ncbi.nlm.nih.gov/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. PMID 30318463. PMC 6309520. https://pubmed.ncbi.nlm.nih.gov/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" (in en). Biochemistry 25 (19): 5408–5414. doi:10.1021/bi00367a010. ISSN 0006-2960. https://pubs.acs.org/doi/abs/10.1021/bi00367a010.
External links
- (protein+ADP-ribosylarginine)+hydrolase at the US National Library of Medicine Medical Subject Headings (MeSH)
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