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Literature summary extracted from

  • Burtscher, H.J.; Klocker, H.; Schneider, R.; Auer, B.; Hirsch-Kauffmann, M.; Schweiger, M.
    ADP-ribosyltransferase from Helix pomatia. Purification and characterization (1987), Biochem. J., 248, 859-864.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.30 3-aminobenzamide 1 mM, 98% inhibition Helix pomatia
2.4.2.30 3-Methoxybenzamide 1 mM, 98% inhibition Helix pomatia
2.4.2.30 Caffeine 1 mM, 23% inhibition Helix pomatia
2.4.2.30 nicotinamide 1 mM, 91% inhibition Helix pomatia
2.4.2.30 Theobromine 1 mM, 76% inhibition Helix pomatia
2.4.2.30 theophylline 1 mM, 72% inhibition Helix pomatia
2.4.2.30 thymidine 1 mM, 70% inhibition Helix pomatia

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.30 0.0267
-
 NAD+
-
 Helix pomatia

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.30 Helix pomatia
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.30 partial Helix pomatia

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.2.30 foot
-
 Helix pomatia
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.2.30 0.0545
-
-
 Helix pomatia

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of histone Helix pomatia nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.2.30 18
-
-
 Helix pomatia

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.2.30 8
-
-
 Helix pomatia