ADP-ribosylhydrolase 1 explained

ADP-ribosylhydrolase 1
Ec Number:3.2.2.19
Cas Number:98668-52-1

(ADP-ribosyl)hydrolase 1, also termed [Protein ADP-ribosylarginine] hydrolase and protein-Nω-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase, 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.[6] The chemical reactions can formally be described as follows:

Nω-(ADP-D-ribosyl)-L-arginyl-[protein] + H2O

\rightleftharpoons

ADP-D-ribose + L-arginyl-[protein]

In addition, the enzyme can reverse the ADP-ribosylation of free arginine:[7] [8]

Nω-(ADP-D-ribosyl)-L-arginine + H2O

\rightleftharpoons

ADP-D-ribose + L-arginine

See also

Notes and References

  1. Moss J, Jacobson MK, Stanley SJ . 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 . 2994036 . 390599 . 10.1073/pnas.82.17.5603 . free .
  2. Moss J, Stanley SJ, Nightingale MS, Murtagh JJ, Monaco L, Mishima K, Chen HC, Williamson KC, Tsai SC . Molecular and immunological characterization of ADP-ribosylarginine hydrolases . The Journal of Biological Chemistry . 267 . 15 . 10481–8 . May 1992 . 10.1016/S0021-9258(19)50043-6 . 1375222 . free .
  3. Konczalik P, Moss J . 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 . 10358013 . 10.1074/jbc.274.24.16736 . free .
  4. Takada T, Iida K, Moss J . Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase . The Journal of Biological Chemistry . 268 . 24 . 17837–43 . August 1993 . 10.1016/S0021-9258(17)46780-9 . 8349667 . free .
  5. Ohno T, Tsuchiya M, Osago H, Hara N, Jidoi J, Shimoyama M . Detection of arginine-ADP-ribosylated protein using recombinant ADP-ribosylarginine hydrolase . Analytical Biochemistry . 231 . 1 . 115–22 . October 1995 . 8678289 . 10.1006/abio.1995.1510 .
  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. 10.1016/j.chembiol.2018.11.001. 2451-9448. 6309922. 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. 10.1016/j.chembiol.2018.09.008. 2451-9448. 6309520. 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. en. 25. 19. 5408–5414. 10.1021/bi00367a010. 3778868 . 0006-2960.

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