Cleavage of thymine glycol by NTHL1 glycosylase

Stable Identifier
Reaction [transition]
Homo sapiens
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NTHL1 (hNTH1; endonuclease III-like protein 1) cleaves oxidized thymine in the form of thymine glycol from DNA sugar-phosphate backbone and acts as a beta lyase to cleave the DNA sugar-phosphate backbone 5' to the apurinic/apyrimidinic (AP) site generated in the glycolysis step (Ikeda et al. 1998, Dizdaroglu et al. 1999, Miyabe et al. 2002).

Literature References
PubMed ID Title Journal Year
9705289 Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease III. Direct identification of Lys-212 as the active nucleophilic residue

Seki, S, Roy, R, Izumi, T, Ikeda, S, Kurosky, A, Sarker, AH, Biswas, T, Boldogh, I, Mitra, S

J. Biol. Chem. 1998
12140329 Identification of 5-formyluracil DNA glycosylase activity of human hNTH1 protein

Zhang, QM, Kino, K, Yasui, A, Yonei, S, Takao, M, Miyabe, I, Sugiyama, H

Nucleic Acids Res. 2002
9890904 Excision of products of oxidative DNA base damage by human NTH1 protein

Sentürker, S, Dizdaroglu, M, Buckley, TJ, Roldán-Arjona, T, Karahalil, B

Biochemistry 1999
Catalyst Activity

oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity of NTHL1:Tg-dsDNA [nucleoplasm]

Orthologous Events
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