Cleavage of thymine by MBD4 glycosylase

Stable Identifier
Reaction [transition]
Homo sapiens
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MBD4 (MED1; methyl-CpG-binding domain protein 4) cleaves thymine mispaired with guanine at CpG islands, which is a consequence of the oxidative deamination of 5-methylcytosine (Petronzelli et al. 2000). The MBD4 catalytic site is located at the C-terminus (Wu et al. 2003). MBD4 may be involved in the maintenance of genomic stability and active DNA demethylation.

Literature References
PubMed ID Title Journal Year
12456671 Mismatch repair in methylated DNA. Structure and activity of the mismatch-specific thymine glycosylase domain of methyl-CpG-binding protein MBD4

Wu, P, Sohail, A, Bhagwat, AS, Zhang, X, Cheng, X, Qiu, C

J. Biol. Chem. 2003
10930409 Biphasic kinetics of the human DNA repair protein MED1 (MBD4), a mismatch-specific DNA N-glycosylase

Yeung, AT, Markham, GD, Stoerker, J, Matsumoto, Y, Bellacosa, A, Riccio, A, Genuardi, M, Seeholzer, SH, Petronzelli, F

J. Biol. Chem. 2000
Catalyst Activity

DNA N-glycosylase activity of MBD4:CpG(T:G)-dsDNA [nucleoplasm]

Orthologous Events
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