Localization of the phosphoester bond hydrolyzed by the major apurinic/apyrmidinic endodeoxyribonuclease from rat-liver chromatin.
The major apurinic/apyrimidinic (AP) endodeoxyribonuclease from rat liver chromatin, an enzyme specific for AP sites in DNA, cleaves the phosphodiester bridge which is the immediate neighbour of the AP site on its 5' side leaving 3'-hydroxyl and 5'-phosphate ends. In contrast with Escherichia coli endonuclease VI, this chromatin enzyme is inactive on reduced AP sites.
D000818:Animals; D001080:Apurinic Acid; D002843:Chromatin / Q000201:enzymology*; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase; D043223:Deoxyribonuclease IV (Phage T4-Induced); D003851:Deoxyribonucleases / Q000378:metabolism*; D004720:Endonucleases / Q000378:metabolism*; D029968:Escherichia coli Proteins; D008099:Liver / Q000201:enzymology*; D010727:Phosphoric Diester Hydrolases; D051381:Rats; D013379:Substrate Specificity
D002843:Chromatin; D029968:Escherichia coli Proteins; D001080:Apurinic Acid; D003851:Deoxyribonucleases; D004720:Endonucleases; D043223:Deoxyribonuclease IV (Phage T4-Induced); C468972:endonuclease IV, E coli; D010727:Phosphoric Diester Hydrolases; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase