Interacting selectively with damaged DNA [goid 3684] [pmid 9223305] [evidence TAS]; Catalysis of the hydrolysis of ester linkages within nucleic acids by creating internal breaks [goid 4519] [pmid 9223305] [evidence TAS]; Interacting selectively with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules) [goid 5515] [pmid 15518571] [evidence IPI]; Interacting selectively with microtubules, filaments composed of tubulin monomers [goid 8017] [evidence IEA]; Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site [goid 8534] [evidence IEA]; Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site [goid 8534] [pmid 10583946] [evidence EXP]; Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site [goid 8534] [pmid 9190902] [evidence TAS]; Catalysis of the hydrolysis of any glycosyl bond [goid 16798] [evidence IEA]; Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring [goid 16829] [evidence IEA]