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Literature summary extracted from

  • Osborne, J.C.; Stanley, S.J.; Moss, J.
    Kinetic mechanisms of two NAD:arginine ADP-ribosyltransferases: the soluble, salt-stimulated transferase from turkey erythrocytes and choleragen, a toxin from Vibrio cholerae (1985), Biochemistry, 24, 5235-5240.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.31 nicotinamide
-
 Meleagris gallopavo

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.31 0.007
-
 NAD+
-
 Meleagris gallopavo
2.4.2.31 0.26
-
 1-(4-aminobutyl)guanidine
-
 Meleagris gallopavo

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.2.31 NAD+ + L-arginine = nicotinamide + Nomega-(ADP-D-ribosyl)-L-arginine + H+ rapid equilibrium random sequential mechanism Meleagris gallopavo
a

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.31 agmatine + NAD+
-
 Meleagris gallopavo nicotinamide + ?
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
2.4.2.31 NAD+
-
 Meleagris gallopavo

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.4.2.31 0.37
-
 nicotinamide
-
 Meleagris gallopavo