DNA-(apurinic or apyrimidinic site) lyase is an enzyme that in humans is encoded by the APEX1gene.
Apurinic/apyrimidinic (AP) sites (also called "abasic sites") occur frequently in DNA molecules by spontaneous hydrolysis, by DNA damaging agents or by DNA glycosylases that remove specific abnormal bases. AP sites are pre-mutagenic lesions that can prevent normal DNA replication. All cells, from simple prokaryotes to humans, have evolved systems to identify and repair such sites. Class II AP endonucleases cleave the phosphodiester backbone 5' to the AP site, thereby initiating a process known as base excision repair (BER). The APEX gene (alternatively named APE1, HAP1, APEN) encodes the major AP endonuclease in human cells. Splice variants have been found for this gene; all encode the same protein.[1]
↑Parker, A; Gu Y; Mahoney W; Lee S H; Singh K K; Lu A L (February 2001). "Human homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair". J. Biol. Chem. United States. 276 (8): 5547–55. doi:10.1074/jbc.M008463200. ISSN0021-9258. PMID11092888.
↑Dianova, I I; Bohr V A; Dianov G L (October 2001). "Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair". Biochemistry. United States. 40 (42): 12639–44. doi:10.1021/bi011117i. ISSN0006-2960. PMID11601988.
Mol CD, Hosfield DJ, Tainer JA (2000). "Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: the 3' ends justify the means". Mutat. Res. 460 (3–4): 211–29. doi:10.1016/s0921-8777(00)00028-8. PMID10946230.
Fritz G, Grösch S, Tomicic M, Kaina B (2003). "APE/Ref-1 and the mammalian response to genotoxic stress". Toxicology. 193 (1–2): 67–78. doi:10.1016/S0300-483X(03)00290-7. PMID14599768.
Tell G, Damante G, Caldwell D, Kelley MR (2005). "The intracellular localization of APE1/Ref-1: more than a passive phenomenon?". Antioxid. Redox Signal. 7 (3–4): 367–84. doi:10.1089/ars.2005.7.367. PMID15706084.
Hung RJ, Hall J, Brennan P, Boffetta P (2006). "Genetic polymorphisms in the base excision repair pathway and cancer risk: a HuGE review". Am. J. Epidemiol. 162 (10): 925–42. doi:10.1093/aje/kwi318. PMID16221808.
Dyrkheeva NS, Khodyreva SN, Lavrik OI (2007). "[Multifunctional human apurinic/apyrimidinic endonuclease 1: the role of additional functions]". Mol. Biol. (Mosk.). 41 (3): 450–66. PMID17685223.
Harrison L, Ascione G, Menninger JC, et al. (1993). "Human apurinic endonuclease gene (APE): structure and genomic mapping (chromosome 14q11.2-12)". Hum. Mol. Genet. 1 (9): 677–80. doi:10.1093/hmg/1.9.677. PMID1284593.
Seki S, Hatsushika M, Watanabe S, et al. (1992). "cDNA cloning, sequencing, expression and possible domain structure of human APEX nuclease homologous to Escherichia coli exonuclease III". Biochim. Biophys. Acta. 1131 (3): 287–99. doi:10.1016/0167-4781(92)90027-w. PMID1627644.
Okazaki T, Chung U, Nishishita T, et al. (1994). "A redox factor protein, ref1, is involved in negative gene regulation by extracellular calcium". J. Biol. Chem. 269 (45): 27855–62. PMID7961715.
Akiyama K, Seki S, Oshida T, Yoshida MC (1994). "Structure, promoter analysis and chromosomal assignment of the human APEX gene". Biochim. Biophys. Acta. 1219 (1): 15–25. doi:10.1016/0167-4781(94)90241-0. PMID8086453.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID8619474.
Chung U, Igarashi T, Nishishita T, et al. (1996). "The interaction between Ku antigen and REF1 protein mediates negative gene regulation by extracellular calcium". J. Biol. Chem. 271 (15): 8593–8. doi:10.1074/jbc.271.15.8593. PMID8621488.
Izumi T, Henner WD, Mitra S (1997). "Negative regulation of the major human AP-endonuclease, a multifunctional protein". Biochemistry. 35 (47): 14679–83. doi:10.1021/bi961995u. PMID8942627.
1e9n: A SECOND DIVALENT METAL ION IN THE ACTIVE SITE OF A NEW CRYSTAL FORM OF HUMAN APURINIC/APYRIMIDINIC ENDONUCLEASE, APE1, AND ITS IMPLICATIONS FOR THE CATALYTIC MECHANISM
1hd7: A SECOND DIVALENT METAL ION IN THE ACTIVE SITE OF A NEW CRYSTAL FORM OF HUMAN APURINIC/APYRIDINIMIC ENDONUCLEASE, APE1, AND ITS IMPLICATIONS FOR THE CATALYTIC MECHANISM