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Literature summary for 2.4.2.31 extracted from

  • Peterson, J.E.; Larew, J.S.A.; Graves, D.J.
    Purification and partial characterization of arginine-specific ADP-ribosyltransferase from skeletal muscle microsomal membranes (1990), J. Biol. Chem., 265, 17062-17069.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol marked decrease in activity, NAD+ and dithiothreitol protects Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Oryctolagus cuniculus
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38500
-
x * 38500, enzyme type beta, SDS-PAGE Oryctolagus cuniculus
39000
-
x * 39000, enzyme type alpha, SDS-PSGE Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
2 enzyme forms: enzyme type alpha and enzyme type beta
-

Purification (Commentary)

Purification (Comment) Organism
enzyme type alpha and enzyme type beta Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginine methyl ester + NAD+
-
Oryctolagus cuniculus nicotinamide + Nomega-(ADP-D-ribosyl)-L-arginine
-
?

Subunits

Subunits Comment Organism
? x * 39000, enzyme type alpha, SDS-PSGE Oryctolagus cuniculus
? x * 38500, enzyme type beta, SDS-PAGE Oryctolagus cuniculus