Reactome | Cleavage of 3-methyladenine by MPG glycosylase

Cleavage of 3-methyladenine by MPG glycosylase

Stable Identifier

R-HSA-110248

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

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Cleavage of 3-methyladenine by MPG glycosylase

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MPG, a 3-methyladenine DNA glycosylase, removes the alkylated DNA base 3-methyladenine (Samson et al. 1991, Vickers et al. 1993, O'Connor 1993). MPG slides along DNA and scans for alkylated bases by inducing cooperative distortions of the double helix that expose nucleotides to the active site of the enzyme (Lau et al. 1998). MPG interacts with both alkylated and unmodified nucleotides and, at a low rate, cleaves unmodified bases (Berdal et al. 1998).

Literature References

PubMed ID	Title	Journal	Year
9430628	Release of normal bases from intact DNA by a native DNA repair enzyme Berdal, KG, Johansen, RF, Seeberg, E	EMBO J.	1998
8475094	Structure of the human 3-methyladenine DNA glycosylase gene and localization close to the 16p telomere Vickers, MA, Vyas, P, Harris, PC, Simmons, DL, Higgs, DR	Proc. Natl. Acad. Sci. U.S.A.	1993
8284199	Purification and characterization of human 3-methyladenine-DNA glycosylase O'Connor, TR	Nucleic Acids Res.	1993
1924375	Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps to chromosome 16 Samson, L, Derfler, B, Boosalis, M, Call, K	Proc. Natl. Acad. Sci. U.S.A.	1991
9790531	Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision Lau, AY, Schärer, OD, Samson, L, Verdine, GL, Ellenberger, T	Cell	1998