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. Author manuscript; available in PMC: 2014 Oct 29.
Published in final edited form as: Biochemistry. 2013 Oct 16;52(43):10.1021/bi401218r. doi: 10.1021/bi401218r

FIGURE 1.

FIGURE 1

Structures of AP, AP-Red, and THF. The authentic AP site exists as an equilibrium between the ring-closed hemiacetal (A) and ring-opened aldehyde (B). The ring-opened aldehyde is subject to β-elimination, and can further be converted to the β,δ-elimination product under basic conditions. The ring-opened aldehyde can be reduced by NaBH4 to generate the AP-Red substrate. APE1 incises the AP site, to create a nick with a 3′-OH and 5′-dRP group.