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Literature summary extracted from

  • Moss, J.; Oppenheimer, N.J.; West, R.E.; Stanley, S.J.
    Amino acid specific ADP-ribosylation: substrate specificity of an ADP-ribosylarginine hydrolase from turkey erythrocytes (1986), Biochemistry, 25, 5408-5414.
    View publication on PubMed

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 ADPribose inhibition by ADPribose stronger than by ADP and AMP Meleagris gallopavo
3.2.2.19 alphaNAD+ inhibition by ADPribose stronger than by alphaNAD+ and betaNAD+ Meleagris gallopavo
3.2.2.19 AMP
-
 Meleagris gallopavo
3.2.2.19 betaNAD+ inhibition by alphaNAD+ stronger than by betaNAD+ 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
3.2.2.19 NaCl inhibition with 200 mM Meleagris gallopavo
3.2.2.19 NaF more than 80% inhibition with 5 mM Meleagris gallopavo

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.2.19 0.0271
-
 ADP-ribosylguanidine
-
 Meleagris gallopavo
3.2.2.19 0.0472
-
 2'-phospho-ADP-ribosylarginine
-
 Meleagris gallopavo
3.2.2.19 0.065
-
 ADP-ribosylarginine
-
 Meleagris gallopavo

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.2.19 40000
-
-
 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 the presence of different enzymes and effectors controlling ADP-ribosylarginine synthesis and degradation is reminiscent of the protein kinase-phosphatase system ADP-ribose + arginine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.19 Meleagris gallopavo
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.2.19 800fold by DE-52, phenyl-Sepharose, carboxymethylcellulose, organomercurial agarose, Ultrogel AcA 54 Meleagris gallopavo

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.2.19 erythrocyte
-
 Meleagris gallopavo
-

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 0.0000476
-
-
 Meleagris gallopavo

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.19 2'-phospho-ADP-ribosylarginine + H2O
-
 Meleagris gallopavo 2'-phospho-ADP-ribose + arginine
-
 ?
3.2.2.19 ADP-ribose-arginine + H2O the presence of different enzymes and effectors controlling ADP-ribosylarginine synthesis and degradation is reminiscent of the protein kinase-phosphatase system Meleagris gallopavo ADP-ribose + arginine
-
 ?
3.2.2.19 ADP-ribose-L-arginine + H2O
-
 Meleagris gallopavo ADP-ribose + L-arginine
-
 ?
3.2.2.19 ADP-ribosylarginine + H2O
-
 Meleagris gallopavo ADP-ribose + L-arginine
-
 ?
3.2.2.19 ADP-ribosylguanidine + H2O at pH less than 7, the enzme exhibits more activity toward ADP-ribosylguanidine than toward ADP-ribosylarginine. The ratio of activity in assays containing ADP-ribosylarginine to those with ADP-ribosylguanidine increases with pH Meleagris gallopavo ADP-ribose + guanidine
-
 ?