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DNA-(apurinic or apyrimidinic site) lyase
・ DNA-3-methyladenine glycosylase
・ DNA-3-methyladenine glycosylase I
・ DNA-3-methyladenine glycosylase II
・ DNA-binding domain
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DNA-(apurinic or apyrimidinic site) lyase : ウィキペディア英語版
DNA-(apurinic or apyrimidinic site) lyase

In enzymology, DNA-(apurinic or apyrimidinic site) lyase, also referred to as DNA-(apurinic or apyrimidinic site) 5'-phosphomonoester-lyase (systematic name) or DNA AP lyase () is a class of enzyme that catalyzes the chemical reaction of the cleavage of the C3'-O-P bond 3' from the apurinic or apyrimidinic site in DNA via beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. In the 1970s, this class of enzyme was found to repair at apurinic or apyrimidinic DNA sites in ''E. coli'' and in mammalian cells. The major active enzymes of this class in bacteria, and specifically, ''E. coli'' is endonuclease type III, while in humans it is a Mg2+-dependent AP endonuclease, APE1. This enzyme encompasses a family of lyases that cleave carbon-oxygen bonds.
Several names for DNA AP lyase include: AP lyase; AP endonuclease class I; endodeoxyribonuclease (apurinic or apyrimidinic); deoxyribonuclease (apurinic or apyrimidinic); E. coli endonuclease III; phage-T4 UV endonuclease; Micrococcus luteus UV endonuclease; AP site-DNA 5'-phosphomonoester-lyase; and X-ray endonuclease III.
==Structural Studies==
Since DNA AP lyase is a class of structures who have numerous target genes that encode for different variations of the enzyme, there is no one single enzyme structure that can be used as an example that encompasses all versions of the enzyme. As of March 2015, (99 ) structures have been solved for this class of enzymes, including 23 PDB accession codes , , , , , , , , , , , , , , , , , , , , , , and . APE1 is a gene that codes for DNA AP lyase in humans which binds to AP DNA loops into both the DNA major and minor grooves and binds a flipped-out AP site in a pocket that excludes DNA bases and racemized-anomer AP sites. Both the APE1 active-site geometry and a complex with cleaved AP-DNA and Mn2+ support a testable structure-based catalytic mechanism. Mn2+ stabilizes the reaction of the lyase activity.〔

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