Article
Pre-steady-state kinetic and mutational insights into mechanisms of endo- and exonuclease DNA processing by mutant forms of human AP endonuclease.
Biochimica et biophysica acta. General subjects - 1 Dec 2022
Bakman Artemiy S, Ishchenko Alexander A, Saparbaev Murat, Fedorova Olga S, Kuznetsov Nikita A
Abstract excerpt
Human apurinic/apyrimidinic endonuclease APE1 catalyzes endonucleolytic hydrolysis of phosphodiester bonds on the 5' side of structurally unrelated damaged nucleotides in DNA or native nucleotides in RNA. APE1 additionally possesses 3'-5'-exonuclease, 3'-phosphodiesterase, and 3'-phosphatase activities. According to structural data, endo- and exonucleolytic cleavage of DNA is executed in different complexes when...
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