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Literature summary for 2.4.2.30 extracted from

  • Bourgeois, C.; Okazaki, I.; Cavanaugh, E.; Nightingale, M.; Moss, J.
    Identification of regulatory domains in ADP-ribosyltransferase-1 that determine transferase and NAD glycohydrolase activities (2003), J. Biol. Chem., 278, 26351-26355.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
DELTA106-288 mutant enzyme has NADase activity, lack of transferase activity Mus musculus
DELTA24–288 signal sequences necessary for export from the ER (at the amino terminus) and addition of a GPI-anchor (at the carboxyl terminus) are deleted. The resulting mutants retain the catalytic properties of the mature wild-type ART1. Their NADase activities relative to transferase activities are very low, and nicotinamide release is enhanced in the presence of the ADP-ribose acceptor, agmatine Mus musculus
DELTA24–293 signal sequences necessary for export from the ER (at the amino terminus) and addition of a GPI-anchor (at the carboxyl terminus) are deleted. The resulting mutants retain the catalytic properties of the mature wild-type ART1. Their NADase activities relative to transferase activities are very low, and nicotinamide release is enhanced in the presence of the ADP-ribose acceptor, agmatine Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ART1 is an arginine-specific transferase Mus musculus ?
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?

Synonyms

Synonyms Comment Organism
ADP-ribosyltransferase-1
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Mus musculus
mono-ADP-ribosyltransferase
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Mus musculus