Reactome | Cleavage of dihydrouracil by NTHL1 glycosylase

Cleavage of dihydrouracil by NTHL1 glycosylase

Stable Identifier

R-HSA-110227

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Cleavage of dihydrouracil by NTHL1 glycosylase

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

NTHL1 (hNTH1; endonuclease III-like protein 1) acts as a DNA glycosylase to cleave 5,6-dihydrouracil, formed by deamination of cytosine with partial saturation of the pyrimidine ring (Dizdaroglu et al. 1993), from the DNA sugar-phosphate backbone, and leaves an apurinic/apyrimidinic (AP) site. After the AP site is created, NTHL1 acts as a beta lyase to cleave the DNA strand 5' to the AP site (Ikeda et al. 1998).

Literature References

PubMed ID	Title	Journal	Year
9705289	Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease III. Direct identification of Lys-212 as the active nucleophilic residue Seki, S, Roy, R, Izumi, T, Ikeda, S, Kurosky, A, Sarker, AH, Biswas, T, Boldogh, I, Mitra, S	J. Biol. Chem.	1998
8218289	Substrate specificity of the Escherichia coli endonuclease III: excision of thymine- and cytosine-derived lesions in DNA produced by radiation-generated free radicals Laval, J, Boiteux, S, Dizdaroglu, M	Biochemistry	1993