Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Ohno, T.; Tsuchiya, M.; Osago, H.; Hara, N.; Jidoi, J.; Shimoyama, M.
    Detection of arginine-ADP-ribosylated protein using recombinant ADP-ribosylarginine hydrolase (1995), Anal. Biochem., 231, 115-122.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.2.19 expression as a glutathione S-transferase-linked fusion protein in Escherichia coli Rattus norvegicus

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 Rattus norvegicus 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 ADP-ribose + arginine
-
 ?
3.2.2.19 ADP-ribose-arginine + H2O Rhodospirillum rubrum 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 ADP-ribose + arginine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.19 Mus musculus
-
-
-
3.2.2.19 Rattus norvegicus
-
-
-
3.2.2.19 Rhodospirillum rubrum
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.2.19 heart
-
 Mus musculus
-
3.2.2.19 heart
-
 Rattus norvegicus
-
3.2.2.19 testis
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.2.19 0.32
-
 as a GST-fusion protein Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Rattus norvegicus ADP-ribose + arginine
-
 ?
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 Rhodospirillum rubrum ADP-ribose + arginine
-
 ?
3.2.2.19 ADP-ribose-L-arginine + H2O as a GST-fusion protein, ADP-ribosylarginine formed by chicken heterophil arginine-specific ADP-ribosyltransferase Rattus norvegicus ADP-ribose + L-arginine
-
 ?
3.2.2.19 casein ADP-ribosylated + H2O
-
 Rattus norvegicus ADP-ribose + casein
-
 ?
3.2.2.19 maltose binding protein ADP-ribosylated + H2O MBP is ADP-ribosylated by an arginine-specific ADP-ribosyltransferase cholera toxin Rattus norvegicus maltose binding protein + ADP-ribose
-
 ?