Cleavage of adenine mispaired with 8-oxoguanine by MUTYH

Stable Identifier
Reaction [transition]
Homo sapiens
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MUTYH (MYH) functions as an adenine DNA glycosylase and removes adenines and 2-hydroxyadenines on the newly synthesized DNA strand mispaired with guanines or 8-oxoguanines on the template strand (Ohtsubo et al. 2000, Boldogh et al. 2001). Under physiological conditions, the preferred substrate for both MUTYH isoforms, MUTYH-3 (alpha-3) and MUTYH-6 (gamma-3) is adenine mispaired with 8-oxoguanine (OGUA:Ade) (Shinmura et al. 2000).

Literature References
PubMed ID Title Journal Year
11121482 Adenine excisional repair function of MYH protein on the adenine:8-hydroxyguanine base pair in double-stranded DNA

Yokota, J, Takeuchi-Sasaki, M, Saitoh, T, Shinmura, K, Nohmi, T, Kim, SR, Yamaguchi, S

Nucleic Acids Res. 2000
11433026 hMYH cell cycle-dependent expression, subcellular localization and association with replication foci: evidence suggesting replication-coupled repair of adenine:8-oxoguanine mispairs

Bassett, H, Milligan, D, Lee, MS, McCullough, AK, Lloyd, RS, Boldogh, I

Nucleic Acids Res. 2001
10684930 Identification of human MutY homolog (hMYH) as a repair enzyme for 2-hydroxyadenine in DNA and detection of multiple forms of hMYH located in nuclei and mitochondria

Nishioka, K, Fujiwara, T, Shimokawa, H, Oda, H, Iwai, S, Ohtsubo, T, Imaiso, Y, Nakabeppu, Y

Nucleic Acids Res. 2000
Catalyst Activity

DNA N-glycosylase activity of MUTYH:(8oxoG:Ade)-dsDNA [nucleoplasm]

Orthologous Events
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