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Literature summary extracted from

  • Moss, J.; Jacobson, M.K.; Stanley, S.J.
    Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme (1985), Proc. Natl. Acad. Sci. USA, 82, 5603-5607.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.2.19 dithiothreitol enhances, activation is maximal with 5-10 mM dithiothreitol and 5-10 mM MgCl2 Meleagris gallopavo

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.2.19 Mg2+ enhances, activation is maximal with 5-10 mM dithiothreitol and 5-10 mM Mg2+ Meleagris gallopavo

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.2.19 ADP-ribose-arginine + H2O Rhodospirillum rubrum
-
 ADP-ribose + arginine
-
 ?
3.2.2.19 ADP-ribose-arginine + H2O Meleagris gallopavo 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 ADP-ribose + arginine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.19 Meleagris gallopavo
-
-
-
3.2.2.19 Rhodospirillum rubrum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.2.19 partial by successive chromatography on DE-52 cellulose, phenyl-Sepharose and organomercurial agarose Meleagris gallopavo

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.2.19 erythrocyte
-
 Meleagris gallopavo
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.19 ADP-ribose-arginine + H2O
-
 Rhodospirillum rubrum ADP-ribose + arginine
-
 ?
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 Meleagris gallopavo ADP-ribose + arginine
-
 ?
3.2.2.19 ADP-ribose-L-arginine + H2O
-
 Meleagris gallopavo ADP-ribose + L-arginine
-
 ?