Eight-Oxoguanine DNA Glycosylase
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Eight-Oxoguanine DNA Glycosylase Definition
The protein 8-Oxoguanine DNA Glycosylase, encoded by the OGG1 gene, is an enzyme in base excision repair. OGG1 incises DNA at 8-oxoguanine residues and excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-n-methylformamidopyrimidine (FAPY) from damaged DNA. OGG1 also has activities of beta-lyase that nicks DNA 3-prime to the lesion and endonuclease that cleaves DNA near apurinic or apyrimidinic sites to products with 5-prime-phosphate. Alternative splicing of the C-terminal region of the OGG1 gene classifies splice variants into two major groups, type 1 and type 2, depending on the last exon of the sequence. Type 1 variants end with exon 7 and type 2 end with exon 8. All variants share the N-terminal region in common (1a/alpha, 1b, 1c, 2a/beta, 2b, 2c, 2d and 2e) and 1a is the prevalent form. OGG1 is ubiquitous and located in nucleus (isoform 1a) and mitochondria (isoform 2a). Defects in OGG1 are associated with tumor formation.
Eight-Oxoguanine DNA Glycosylase Synonyms
8-Oxoguanine DNA Glycosylase, N-Glycosylase/DNA Lyase, OGG1
Terms in Eight-Oxoguanine DNA Glycosylase category
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