Cleavage of 3-methyladenine by MPG glycosylase

Stable Identifier
R-HSA-110248
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
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

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
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
9430628 Release of normal bases from intact DNA by a native DNA repair enzyme

Berdal, KG, Johansen, RF, Seeberg, E

EMBO J. 1998
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
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
DNA N-glycosylase activity of MPG:MADE-dsDNA [nucleoplasm]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created
Cite Us!