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Literature summary for 2.4.2.31 extracted from

  • Banasik, M.; Stedeford, T.; Strosznajder, R.P.; Hsu, C.H.; Tanaka, S.; Ueda, K.
    Differential effects of heterocyclic amines on poly(ADP-ribose) polymerase-1 and mono-ADP-ribosyltransferase A (2006), J. Physiol. Pharmacol., 57 Suppl 4, 15-22.
    View publication on PubMed
Search for more literature for 2.4.2.31

Activating Compound

Activating Compound Comment Organism Structure
3-amino-1-methyl-5H-pyrido[4,3-b]indole i.e. Trp-P-2, 71% activation at 3 mM Meleagris sp.

Inhibitors

Inhibitors Comment Organism Structure
3-amino-1,4-dimethyl-5H-pyrido[4,3-b]indole i.e. Trp-P-1, 53% inhibition at 5 mM, IC50: 2.8 mM Meleagris sp.
additional information comparison of the effects of heterocyclic amines acting as potent carcinogens on poly(ADP-ribose) polymerase-1, PARP-1, EC 2.4.2.30, and the arginine-specific mono-ADP-ribosyltransferase A, overview Meleagris sp.

Organism

Organism UniProt Comment Textmining
Meleagris sp.
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
 Meleagris sp.
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
histone H2B + NAD+
-
 Meleagris sp. Nomega-[(2'-phospho-ADP)-D-ribosyl]-histone H2B-L-arginine + nicotinamide
-
 ?
additional information the enzyme is involved in signal transduction and cytoskeletal realignment Meleagris sp. ?
-
 ?

Synonyms

Synonyms Comment Organism
arginine-specific mono-ADP-ribosyltransferase A
-
 Meleagris sp.
MART-A
-
 Meleagris sp.
mono-ADP-ribosyltransferase A
-
 Meleagris sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Meleagris sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Meleagris sp.

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.8
-
 i.e. Trp-P-1, 53% inhibition at 5 mM, IC50: 2.8 mM Meleagris sp. 3-amino-1,4-dimethyl-5H-pyrido[4,3-b]indole