EC Number   |
Natural Substrates |
|---|
   3.2.2.19 | 2'-O-acetyl-ADP-ribose + H2O |
- |
| 3.2.2.19 | ADP-ribose-arginine + H2O |
- |
| 3.2.2.19 | ADP-ribose-arginine + H2O |
in Rhodospirillium rubrum, a nitrogen-fixing microorganism, ADP-ribosylation of an arginine residue in a nitrogenase inhibits its activity. Inactivation of the nitrogenase can be reversed by a hydrolase which cleaves the ADP-ribose-arginine bond |
| 3.2.2.19 | ADP-ribose-arginine + H2O |
the presence of ADP-ribosyltransferases and ADP-ribosylhydrolases may lead to an ADP-ribosylation/de-ADP-ribosylation cycle, lending further support to the hypothesis that this covalent modification may have a regulatory function in animal cells |
| 3.2.2.19 | ADP-ribose-arginine + H2O |
the presence of ecto-ADP-ribosyltransferase and arginine-specific ADP-ribosylation of cell-surface protein have been reported. Application of the method on the extracellular ADP-ribosylation of intact cells may help to reveal the role of the modification in physiological events such as cell adhesion or cell-cell communication |
| 3.2.2.19 | ADP-ribose-arginine + H2O |
ADP-ribosylarginine hydrolase presumably regenerates an arginine site that can be ADP-ribosylated by NAD-arginine ADP-ribosyltransferase. The balance between these two opposing enzymatic activities may control some aspects of cellular metabolism |
| 3.2.2.19 | ADP-ribose-arginine + H2O |
in nitrogen fixing bacteria, Rhodospirillium rubrum, ADP-ribosylation-de-ADP-ribosylation of a specific arginine-residue of dinitrogenase reductase has been shown to regulate the enzyme activity |
| 3.2.2.19 | ADP-ribose-arginine + H2O |
the existence of a ADP-ribosylation cycle was established in the bacterium Rhodospirillium rubrum where it regulates dinitrogenase reductase, a key enzyme in nitrogen fixation |
| 3.2.2.19 | ADP-ribose-arginine + H2O |
the presence of different enzymes and effectors controlling ADP-ribosylarginine synthesis and degradation is reminiscent of the protein kinase-phosphatase system |
| 3.2.2.19 | more |
ADPRH cleaves the glycosidic bond of ADP-ribose attached to an Arg residue of a protein |
