Cleavage of adenine mispaired with 8-oxoguanine by MUTYH

Stable Identifier
R-HSA-110246
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
11433026 hMYH cell cycle-dependent expression, subcellular localization and association with replication foci: evidence suggesting replication-coupled repair of adenine:8-oxoguanine mispairs

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

Nucleic Acids Res. 2001
11121482 Adenine excisional repair function of MYH protein on the adenine:8-hydroxyguanine base pair in double-stranded DNA

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

Nucleic Acids Res. 2000
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

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

Nucleic Acids Res. 2000
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
DNA N-glycosylase activity of MUTYH:(8oxoG:Ade)-dsDNA [nucleoplasm]
Physical Entity
Activity
Orthologous Events
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