Literature summary for 3.2.2.27 extracted from

Cole, H.A.; Tabor-Godwin, J.M.; Hayes, J.J.
Uracil DNA glycosylase activity on nucleosomal DNA depends on rotational orientation of targets (2010), J. Biol. Chem., 285, 2876-2885.

Search for more literature for 3.2.2.27

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	uracil DNA glycosylase activity on nucleosomal DNA depends on rotational orientation of targets	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	association of linker histone reduces activity of UDG at selected sites near where the globular domain of H1 is proposed to bind to the nucleosome as well as within the extra-core DNA	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P12295	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	preparation of a set of model nucleosome substrates, of 154mer DNA, in which single thymidine residues are replaced with uracil at specific locations and a second set of nucleosomes in which uracils are randomly substituted for all thymidines. UDG efficiently removes uracil from internal locations in the nucleosome where the DNA backbone is oriented away from the surface of the histone octamer, without significant disruption of histone-DNA interactions. However, uracils at sites oriented toward the histone octamer surface are excised at much slower rates, consistent with a mechanism requiring spontaneous DNA unwrapping from the nucleosome. In contrast to the nucleosome core, UDG activity on DNA outside the core DNA region is similar to that of naked DNA, overview	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
UDG	-	Escherichia coli
uracil DNA glycosylase	-	Escherichia coli

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Release 2023.1 (January 2023)