NUDT15 dimer dephosphorylates 6TdGTP to 6TdGMP

Stable Identifier
Reaction [transition]
Homo sapiens
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Nucleotide triphosphate diphosphatase (NUDT15) is thought to catalyze the hydrolysis of nucleoside triphosphates, including the prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP, and stops their incorporation into DNA and RNA respectively (Kasumi et al. 1993, Carter et al. 2015, Hashiguchi et al. 2018). Polymorphisms in NUDT15 are associated with thiopurine intolerance in Asian populations (Tanaka & Saito 2021). Defective NUDT15 alleles show excessive levels of thiopurine active metabolites and toxicity (Moriyama et al. 2016).
Literature References
PubMed ID Title Journal Year
26238318 Crystal structure, biochemical and cellular activities demonstrate separate functions of MTH1 and MTH2

Valerie, NC, Gustafsson, R, Gad, H, Stenmark, P, Desroses, M, Hagenkort, A, Page, BD, Jemth, AS, Griese, JJ, Helleday, T, Boström, J, Carter, M, Warpman Berglund, U

Nat Commun 2015
29482072 The roles of human MTH1, MTH2 and MTH3 proteins in maintaining genome stability under oxidative stress

Umezu, K, Hayashi, M, Sekiguchi, M, Hashiguchi, K

Mutat Res 2018
8226881 Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis

Tsuzuki, T, Kakuma, T, Furuichi, M, Maki, H, Kawabata, S, Sekiguchi, M, Sakumi, K

J. Biol. Chem. 1993
Event Information
Catalyst Activity

8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity of NUDT15 dimer [cytosol]

Orthologous Events
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