Reactome | NUDT15 dimer dephosphorylates 6TdGTP to 6TdGMP

NUDT15 dimer dephosphorylates 6TdGTP to 6TdGMP

Stable Identifier

R-HSA-9750555

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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NUDT15 dimer dephosphorylates 6TdGTP to 6TdGMP

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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