In molecular biology, the (ADP-ribosyl)hydrolase (ARH) family contains enzymes which catalyses the hydrolysis of ADP-ribosyl modifications from proteins, nucleic acids and small molecules.
Types This family has three members in humans (ARH1-3): ARH1, also termed [Protein ADP-ribosylarginine] hydrolase, cleaves ADP-ribose-L-arginine, ARH2, which is predicted to be enzymatically inactive, and ARH3, which cleaves primarily ADP-ribose-L-serine, but was shown to also hydrolyse poly(ADP-ribose), 1''-O-acetyl-ADP-ribose and alpha-nicotinamide adenine dinucleotide. The family also includes ADP-ribosyl-(dinitrogen reductase) hydrolase (DraG) known to regulate dinitrogenase reductase, a key enzyme of the nitrogen fixating pathway in bacteria, and most surprisingly jellyfish crystallins, although the latter proteins appear to have lost the presumed active site residues. Class Species Intracellularlocation Activity Function Bacteria Human Others I ARH1 endoplasmic reticulum, cytoplasm ADP-ribosylarginine hydrolase inflammation, genomic stability II ARH2 cytoplasm, cardiac sarcomeres inactive heart chamber outgrowth III ARH3 Nucleus, cytoplasm ADP-ribosylserine hydrolase DNA repair IV Crystallin J1 and SelJ inactive Crystallin V DraG ADP-ribosylarginine hydrolase Regulation of nitrogen fixation
See also ADP-ribosylhydrolase 1 ADP-ribosyl-(dinitrogen reductase) hydrolase
References