(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] + H2 O ⇌ {\displaystyle \rightleftharpoons } 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 + H2 O ⇌ {\displaystyle \rightleftharpoons } ADP-D -ribose + L-arginine ^ 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 .
Activity Regulation Classification Kinetics Types