Biochemistry (Moscow)

, Volume 81, Issue 9, pp 951–967 | Cite as

AP endonuclease 1 as a key enzyme in repair of apurinic/apyrimidinic sites

  • N. S. Dyrkheeva
  • N. A. Lebedeva
  • O. I. LavrikEmail author


Human apurinic/apyrimidinic endonuclease 1 (APE1) is one of the key participants in the DNA base excision repair system. APE1 hydrolyzes DNA adjacent to the 5′-end of an apurinic/apyrimidinic (AP) site to produce a nick with a 3′-hydroxyl group and a 5′-deoxyribose phosphate moiety. APE1 exhibits 3′-phosphodiesterase, 3′-5′-exonuclease, and 3-phosphatase activities. APE1 was also identified as a redox factor (Ref-1). In this review, data on the role of APE1 in the DNA repair process and in other metabolic processes occurring in cells are analyzed as well as the interaction of this enzyme with DNA and other proteins participating in the repair system.


human apurinic/apyrimidinic endonuclease 1 (APE1) AP site base excision repair protein–DNA interactions protein–protein interactions 



DNA containing AP site


apurinic/apyrimidinic endonuclease 1

AP site

apurinic/apyrimidinic site


base excision repair


base pairs


deoxyribose phosphate

F (tetrahydrofuran)





flap endonuclease 1




nucleotide excision repair


homolog 1 of endonuclease III


8oxoguanine-DNA glycosylase




poly(ADP-ribose)polymerase 1


proliferating cell nuclear antigen


5′-tetrahydrofuran phosphate


polynucleotide kinase-phosphatase

Pol β

DNA polymerase β




tyrosyl-DNA phosphodiesterase 1


human X-ray repair cross-complementing protein 1


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Copyright information

© Pleiades Publishing, Ltd. 2016

Authors and Affiliations

  • N. S. Dyrkheeva
    • 1
  • N. A. Lebedeva
    • 1
    • 2
  • O. I. Lavrik
    • 1
    • 2
    • 3
    Email author
  1. 1.Institute of Chemical Biology and Fundamental MedicineSiberian Division of the Russian Academy of SciencesNovosibirskRussia
  2. 2.Novosibirsk State UniversityNovosibirskRussia
  3. 3.Altai State UniversityBarnaulRussia

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