ADP-ribosylhydrolase 1

(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
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
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

See also

References
  1. 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.
  2. 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.
  3. 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.
  4. 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.
  5. 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.
  6. 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.
  7. 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.
  8. 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.
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