Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.2.30 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

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Helix pomatia
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Helix pomatia

Source Tissue

Source Tissue Comment Organism Textmining
foot
-
Helix pomatia
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Helix pomatia