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- W76810399 abstract "Apurinic/Apyrimidinic (AP) sites arise spontaneously in DNA even at neutral pH owing to the inherent lability of the N-glycosyl bond. This lability is a consequence of the absence of the sugar 2′ oxygen in DNA compared to RNA. It has been calculated that up to 10,000 bases (primarily purines) are lost per human cell per day (reviewed in 3,18,39,40,68). Because unrepaired AP sites are potentially both cytotoxic and mutagenic (noncoding), this burden of damage to DNA represents one of the major threats to viability and genome stability in human cells. AP sites in DNA can also arise either by the actions of reactive oxygen species (ROS), or by enzymatic excision of damaged bases via the cleavage of the N-glycosyl bond catalyzed by a DNA glycosylase. AP sites in double-stranded DNA are recognized by a class of enzymes termed AP endonucleases that cleave the phosphodiester backbone on the 5′ side of the AP site via a hydrolytic mechanism and hence catalyze the initial step in AP site repair (reviewed in 3,18,68). A number of DNA glycosylases exhibit AP site-cleavage activity as part of their mechanism of action. However these enzymes act as β-elimination catalysts, cleaving the phosphodiester backbone 3’ to the AP site. This class of enzyme (so-called class I AP endonucleases) will not be discussed further in this chapter. Instead we direct readers to recent reviews containing a discussion of the properties of these enzymes (13,14,22,37,45,59,69)." @default.
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- W76810399 date "2001-01-01" @default.
- W76810399 modified "2023-09-23" @default.
- W76810399 title "Structure and Functions of the Major Human AP Endonuclease HAP1/Ref-1" @default.
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- W76810399 doi "https://doi.org/10.1007/978-1-59259-095-7_4" @default.
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