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• W2060801142 abstract "N-Methylpurine-DNA glycosylase (MPG), a ubiquitous DNA repair protein, removes several N-alkylpurine adducts, hypoxanthine, cyclic ethenoadducts of adenine, guanine and cytosine and 8-oxoguanine from DNA. The recombinant human and mouse MPGs, purified from Escherichia coli, show a significant difference in substrate preference. While both proteins prefer 3-methyladenine over other N-alkylpurines in DNA, the mouse MPG removes 7-methylguanine and 3-methylguanine at an approximately 2- to 3-fold higher rate than the human protein when adjusted for equal activity for the release of 3-methyladenine from DNA. Hybrid recombinant proteins containing N-terminal and C-terminal halves of the human and mouse glycosylases were partially purified from MPG-negative E.coli. Their substrate preferences suggest that the N-terminal half is more critical for the recognition of 3-methylguanine and 7-methylguanine." @default.
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• W2060801142 date "1996-01-01" @default.
• W2060801142 modified "2023-10-14" @default.
• W2060801142 title "Distinct substrate preference of human and mouse N-methylpurine-DNA glycosylases" @default.
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• W2060801142 doi "https://doi.org/10.1093/carcin/17.10.2177" @default.
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