ADP-ribosylarginine hydrolase (ADPRH)

ADP-ribosylarginine hydrolase (ADPRH) is a cytoplasmic enzyme responsible for specifically and efficiently hydrolyzing the N-glycosidic bond between ADP-ribose and arginine residues in proteins[1][5][7]. This reaction reverses mono-ADP-ribosylation, a critical posttranslational modification that controls protein function in cellular signaling, response to toxins, and potentially in tumor suppression. ADPRH is ubiquitously expressed and has negligible activity on other ADP-ribosyl linkages (e.g., serine, glutamate). Deficiency or mutation of ADPRH leads to abnormal cell proliferation and increased risk of multiple cancer types, and it may influence cellular defense against bacterial exotoxins[3][1]. While ADPRH and related hydrolases have emerged as research targets in oncology and infectious diseases, there are not yet clinically available inhibitors specific to ADPRH.

Other names

ARH1ADP-ribosylhydrolase ARH1hARH1ADP-ribose-L-arginine cleaving enzyme[Protein ADP-ribosylarginine] hydrolase

Removal (hydrolysis) of mono-ADP-ribose from arginine residues of proteins, reversing arginine-specific ADP-ribosylation[1][5][7]