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

BRENDA support

Literature summary extracted from

  • Takada, T.; Okazaki, I.J.; Moss, J.
    ADP-Ribosylarginine hydrolases (1994), Mol. Cell. Biochem., 138, 119-122.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.2.19 dithiothreitol
-
Mus musculus
3.2.2.19 dithiothreitol
-
Rattus norvegicus
3.2.2.19 dithiothreitol activated by Mg2+ and dithiothreitol Meleagris gallopavo

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
3.2.2.19 expression in Escherichia coli Mus musculus
3.2.2.19 wild-type and mutant rat hydrolases are expressed in Escherichia coli Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.2.19 ADP inhibition by ADP stronger than by AMP Meleagris gallopavo
3.2.2.19 ADP
-
Rattus norvegicus
3.2.2.19 ADPribose inhibition by ADPribose stronger than by ADP and AMP Meleagris gallopavo
3.2.2.19 ADPribose
-
Oryctolagus cuniculus
3.2.2.19 ADPribose
-
Rattus norvegicus
3.2.2.19 AMP
-
Meleagris gallopavo
3.2.2.19 dithiothreitol incubation in 20 mM at 37°C leads to rapid loss of activity but addition of Mg2+ stabilizes the hydrolase against thermal inactivation Meleagris gallopavo

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.2.19 Mg2+
-
Meleagris gallopavo
3.2.2.19 Mg2+
-
Mus musculus
3.2.2.19 Mg2+
-
Rattus norvegicus
3.2.2.19 Mg2+
-
Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.2.19 39000
-
-
Mus musculus
3.2.2.19 39000
-
-
Rattus norvegicus
3.2.2.19 39000
-
gel filtration, SDS-PAGE 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 Meleagris gallopavo
-
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 Meleagris gallopavo
-
-
-
3.2.2.19 Mus musculus
-
-
-
3.2.2.19 Oryctolagus cuniculus
-
-
-
3.2.2.19 Ovis aries
-
-
-
3.2.2.19 Rattus norvegicus
-
-
-
3.2.2.19 Rhodospirillum rubrum
-
-
-
3.2.2.19 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.2.19 20000 fold by DE-52, phenyl-Sepharose, hydroxylapatite, Affi-Gel 501 organo-mercurial agarose, Ultrogel AcA 54 Rattus norvegicus
3.2.2.19 200000fold by DE-52, phenyl-Sepharose, hydroxylapatite, Ultrogel AcA 54, Mono Q chromatography Meleagris gallopavo
3.2.2.19 partial Mus musculus
3.2.2.19 partial Sus scrofa
3.2.2.19 partial Oryctolagus cuniculus
3.2.2.19 partial Ovis aries
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
-
3.2.2.19 fibroblast
-
Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.19 ADP-ribose-arginine + H2O
-
Meleagris gallopavo 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 histones ADP-ribosylated + H2O
-
Mus musculus ?
-
?
3.2.2.19 lysozyme ADP-ribosylated + H2O
-
Rattus norvegicus ?
-
?

Subunits

EC Number Subunits Comment Organism
3.2.2.19 monomer 1 * 39000, SDS-PAGE Meleagris gallopavo