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Literature summary for 3.2.2.19 extracted from

  • Moss, J.; Tsai, S.C.; Adamik, R.; Chen, H.C.; Stanley, S.J.
    Purification and characterization of ADP-ribosylarginine hydrolase from turkey erythrocytes (1988), Biochemistry, 27, 5819-5823.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
N-ethylmaleimide after incubation with dithiothreitol at 30°C the thiol-sensitive and the thiol-resistant hydrolase are inactivated by NEM at 4°C , exposure to dithiothreitol at 4°C is sufficient to permit subsequent inactivation of the thiol-sensitive but not the thiol-resistant form by NEM Meleagris gallopavo
NAD+ 10 mM Mg2+ or 10 mM Mg2+ plus 5 mM dithiothreitol reduces the extent of inactivation of thiol-sensitive and thiol-resistant hydrolase by NAD+ Meleagris gallopavo
NAD-arginine ADP-ribosyltransferase 10 mM Mg2+ or 10 mM Mg2+ plus 5 mM dithiothreitol reduces the extent of inactivation of thiol-sensitive and thiol-resistant hydrolase by NAD-arginine ADP-ribosyltransferase Meleagris gallopavo

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39000
-
gel filtration, SDS-PAGE Meleagris gallopavo

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Meleagris gallopavo
-
-
-
Rhodospirillum rubrum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
200000fold by DE-52, phenyl-Sepharose, hydroxylapatite, Ultrogel AcA 54, Mono Q chromatography Meleagris gallopavo
depending on the procedure used for purification, either a thiol-resistant or a thiol-sensitive species can be isolated. Organomercurial chromatography apparently results in the formation of the thiol-sensitive species of hydrolase as the exposure of the thiol-resistant form to HgCl2 does Meleagris gallopavo

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
Meleagris gallopavo
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0000395
-
thiol-sensitive form Meleagris gallopavo
0.0000487
-
thiol-resistant form Meleagris gallopavo

Substrates and Products (Substrate)

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

Subunits

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