3.2.2.23	2,6-diamino-4-hydroxy-5-formamidopyrimidine-DNA + H2O	-	
3.2.2.23	2,6-diamino-4-hydroxy-5-formamidopyrimidine:Cyt oligodeoxynucleotide + H2O	-	
3.2.2.23	2,6-diamino-4-hydroxy-5-formamidopyrimidine:Cyt-DNA + H2O	-	
3.2.2.23	5,6-dihydrouracil-DNA + H2O	DHU is excised from DNA by a number of DNA glycosylases including Fpg and Nei	
3.2.2.23	8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide + H2O	-	
3.2.2.23	8-oxo-7,8-dihydroguanine:Cyt-DNA + H2O	-	
3.2.2.23	DNA + H2O	removes oxidized purines from oxidatively damaged DNA	
3.2.2.23	DNA + H2O	catalyzes the initial steps in the repair of DNA containing oxidized purines	
3.2.2.23	DNA + H2O	DNA repair enzyme specific for the removal of purine-derived lesions from DNA damaged by free radicals and other oxidative processes	
3.2.2.23	DNA + H2O	plays an important role in base excision repair of oxidatively damaged DNA	
3.2.2.23	DNA + H2O	involved in the repair of oxidized purines generated in the genome by endogenous or exogenous oxidative stress	
3.2.2.23	DNA + H2O	involved in replication-associated repair of oxidized bases	
3.2.2.23	DNA + H2O	important role in protecting DNA against oxidative free radicals and reactive oxygen-derived species	
3.2.2.23	DNA + H2O	biological substrates are purine oxidation products	
3.2.2.23	DNA + H2O	DNA base excision repair enzyme	
3.2.2.23	DNA + H2O	bifunctional base excision repair enzyme: DNA glycosylase/AP lyase	
3.2.2.23	DNA containing 2,6-diamino-4-hydroxyformamidopyrimidine residues + H2O	repair of the major DNA lesions 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxyformamidopyrimidine formed by reactive oxidative species	
3.2.2.23	DNA containing 7-hydro-8-oxoguanine + H2O	repairs oxidative DNA damage by efficiently removing formamidopyrimidine lesions and 8-oxoguanine residues from DNA	
3.2.2.23	DNA containing 7-hydro-8-oxoguanine + H2O	dublex, primary physiological substrate, DNA repair	
3.2.2.23	DNA containing 8-hydroxyguanine residues + H2O	natural substrate: 7,8-dihydro-8-oxo-dG, DNA base excision repair	
3.2.2.23	DNA containing 8-hydroxyguanine residues + H2O	dublex, primary physiological substrate is 7,8-dihydro-8-oxoguanine-DNA, DNA repair	
3.2.2.23	DNA containing 8-hydroxyguanine residues + H2O	repair of the major DNA lesions 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxyformamidopyrimidine formed by reactive oxidative species	
3.2.2.23	DNA containing 8-oxo-2'-deoxyguanosine residues + H2O	-	
3.2.2.23	DNA containing 8-oxoguanine residues + H2O	-	
3.2.2.23	DNA containing 8-oxoguanine residues + H2O	best substrate	
3.2.2.23	DNA containing ring-opened N7-methylguanine + H2O	repairs oxidative DNA damage by efficiently removing formamidopyrimidine lesions and 8-oxoguanine residues from DNA	
3.2.2.23	additional information	base excision repair initiated by the enzyme is less effective in the first two days of growth and more effective later in stationary phase	
3.2.2.23	additional information	enzyme mediates repair of lesions containing hydantoins in vivo	
3.2.2.23	additional information	8-oxo-7,8-dihydroguanine, i.e. 8-oxoGua, and 2,6-diamino-4-hydroxy-5-formamidopyrimidine, i.e. FapyGua, are premutagenic DNA lesions that appear in DNA damaged by reactive oxygen species of endogenous and environmental origin, and are excised from DNA by the enzyme. The fidelity of the 8-oxoGua repair system depends on discrimination between 8-oxoGua:Cyt and 8-oxoGua:Ade pairs by OGG1	
3.2.2.23	additional information	defective repair of 5-hydroxy-2-deoxycytidine in Cockayne syndrome cells is complementated by Escherichia coli formamidopyrimidine DNA glycosylase and endonuclease III	
3.2.2.23	additional information	formamidopyrimidine-DNA N-glycosylase operates in the base excision repair pathway in bacteria by removing oxidized guanine bases from DNA and can also cleave the nascent or preformed abasic DNA by beta,delta-elimination. The cleaved product formation is initially reversible	
3.2.2.23	additional information	FPG excises oxidatively damaged purines in the base excision repair pathway, overview	
3.2.2.23	additional information	MmuNeil3 is a bifunctional DNA glycosylase that recognizes spiroiminodihydantoin and guanidinohydantoin, as well as 2,6-diamino-4-hydroxy-5-formamidopyrimidine, and 4,6-diamino-5-formamidopyrimidine, in double-stranded substrates. Neil3 greatly reduces both the spontaneous mutation frequency and the level of 2,6-diamino-4-hydroxy-5-formamidopyrimidine in the DNA. Substrate specificity of MmuNeil3 in vivo, overview	
3.2.2.23	additional information	NEIL1 is active on DNA lesions in ssDNA, particularly in the context of a single-stranded bubble in a duplex sequence