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Oxygen radicals damage chromosonal DNA causing cell death and inducing mutations. Although a major focus of oxidatively damaged DNA has centered on the repair of 8-oxo-G, a number of other damaged DNA sites are created by free-radical attack on DNA. The human NTH1 repair protein is one enzyme that has been shown to act on a large number of these other oxidatively damaged DNA sites.A homologue of E. coli Endonuclease III, NTH is a DNA glycosylase with apurinic/apyrimidinic lyase activity. The NTH protein has broad substrate specificity, including numerous ring saturation and fragmentation products of pyrimidines. Research indicates NTH plays a crucial role in removal of oxidative base lesions in mitochondrial DNA.
bifunctional DNA N-glycoslyase/DNA-(apurinic or apyrimidinic site) lyase; Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase; DNA glycoslyase/AP lyase; DNA glycosylase/AP lyase; Endonuclease III-like protein 1; FAP3; hNTH1; nth (endonuclease III)-like 1 (E.coli); nth endonuclease III-like 1; Nth1; NTHL 1; Nthl1; nth-like DNA glycosylase 1; OCTS 3; OCTS3; thymine glycol DNA glycosylase/AP lyase
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