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Literature summary for 2.4.2.30 extracted from

  • De Murcia, G.; Huletsky, A.; Poirier, G.G.
    Modulation of chromatin structure by poly(ADP-ribosyl)ation (1988), Biochem. Cell Biol., 66, 626-635.
    View publication on PubMed
Search for more literature for 2.4.2.30

Activating Compound

Activating Compound Comment Organism Structure
DNA the enzyme is completely dependent on the presence of DNA containing single or double stranded breaks. Activation results in a decondensation of chromatin superstructure in vitro, which is caused mainly by hyper(ADP-ribosyl)ation of histone H1 Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
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 Bos taurus 5634
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bos taurus cuts produced in vivo on DNA during DNA repair activate the enzyme, which then synthesiszes poly(ADP-ribose) on histone H1, in particular, and contributes to the opening of the 25 nm chromatin fiber, resulting in the increased accessibility of DNA to excision repair enzymes ?
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Organism

Organism UniProt Comment Textmining
Bos taurus
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information cuts produced in vivo on DNA during DNA repair activate the enzyme, which then synthesiszes poly(ADP-ribose) on histone H1, in particular, and contributes to the opening of the 25 nm chromatin fiber, resulting in the increased accessibility of DNA to excision repair enzymes Bos taurus ?
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 ?
NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of histone H1 Bos taurus nicotinamide + (ADP-D-ribosyl)n+1-acceptor
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 ?