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Literature summary extracted from

  • Kim, E.S.; Graves, D.J.
    Development of a high-performance liquid chromatography assay method and characterization of adenosine diphosphate-ribosylarginine hydrolase in skeletal muscle (1990), Anal. Biochem., 187, 251-257.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.2.19 dithiothreitol
-
 Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.2.19 ADPribose 80% inhibition with 2 mM ADPribose Gallus gallus
3.2.2.19 ADPribose 80% inhibition with 2 mM ADPribose Oryctolagus cuniculus
3.2.2.19 ADPribose 80% inhibition with 2 mM ADPribose Rattus norvegicus
3.2.2.19 Arginine methyl ester 15% inhibition with 2 mM arginine methyl ester Gallus gallus
3.2.2.19 Arginine methyl ester 15% inhibition with 2 mM arginine methyl ester Oryctolagus cuniculus
3.2.2.19 Arginine methyl ester 15% inhibition with 2 mM arginine methyl ester Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.2.19 0.0053
-
 ADP-ribose DABSYL-L-arginine methyl ester in presence of 15 mM magnesium and 5 mM DTT Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.2.19 Mg2+
-
 Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.2.19 40000
-
 gel filtration Gallus gallus
3.2.2.19 40000
-
 gel filtration Rattus norvegicus
3.2.2.19 40000
-
 gel filtration Oryctolagus cuniculus

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 Gallus gallus ADP-ribosylarginine hydrolase presumably regenerates an arginine site that can be ADP-ribosylated by NAD-arginine ADP-ribosyltransferase. The balance between these two opposing enzymatic activities may control some aspects of cellular metabolism 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 Gallus gallus
-
-
-
3.2.2.19 Oryctolagus cuniculus
-
-
-
3.2.2.19 Rattus norvegicus
-
-
-
3.2.2.19 Rhodospirillum rubrum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.2.19 homogenate of chicken muscle cells from tissue culture was centrifugated and the supernatant dialyzed Gallus gallus
3.2.2.19 partial Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.2.19 brain
-
 Rattus norvegicus
-
3.2.2.19 brain
-
 Oryctolagus cuniculus
-
3.2.2.19 heart
-
 Rattus norvegicus
-
3.2.2.19 kidney
-
 Rattus norvegicus
-
3.2.2.19 liver
-
 Rattus norvegicus
-
3.2.2.19 muscle
-
 Gallus gallus
-
3.2.2.19 muscle
-
 Rattus norvegicus
-
3.2.2.19 muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.19 ADP-ribose DABSYL-L-arginine methyl ester + H2O
-
 Gallus gallus DABSYL-L-arginine methyl ester + ADP-ribose
-
 ?
3.2.2.19 ADP-ribose DABSYL-L-arginine methyl ester + H2O
-
 Rattus norvegicus DABSYL-L-arginine methyl ester + ADP-ribose
-
 ?
3.2.2.19 ADP-ribose DABSYL-L-arginine methyl ester + H2O
-
 Oryctolagus cuniculus DABSYL-L-arginine methyl ester + ADP-ribose
-
 ?
3.2.2.19 ADP-ribose-arginine + H2O ADP-ribosylarginine hydrolase presumably regenerates an arginine site that can be ADP-ribosylated by NAD-arginine ADP-ribosyltransferase. The balance between these two opposing enzymatic activities may control some aspects of cellular metabolism Gallus gallus 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
-
 ?