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NH2-terminal proline acts as a nucleophile in the glycosylase/AP-lyase reaction catalyzed by Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg) protein.
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Substrate specificity of Escherichia coli MutY protein.
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Base excision of oxidative purine and pyrimidine DNA damage in Saccharomyces cerevisiae by a DNA glycosylase with sequence similarity to endonuclease III from Escherichia coli.
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Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily.
Curr Biol. 1996 Aug 1;6(8):968-80. doi: 10.1016/s0960-9822(02)00641-3.
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Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine.
Proc Natl Acad Sci U S A. 1996 May 28;93(11):5197-202. doi: 10.1073/pnas.93.11.5197.
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3'- and 5'-strand cleavage reactions catalyzed by the Fpg protein from Escherichia coli occur via successive beta- and delta-elimination mechanisms, respectively.
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Repair of 8-hydroxyguanine in DNA by mammalian N-methylpurine-DNA glycosylase.
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Mutagenesis by 8-oxoguanine: an enemy within.
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