2-Hidroksi-dATP difosfataza
(Preusmjereno sa stranice MTH2)
2-Hidroksi-dATP difosfataza | |||||||||
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Identifikatori | |||||||||
EC broj | 3.6.1.56 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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2-Hidroksi-dATP difosfataza (EC 3.6.1.56, NUDT1, MTH1, MTH2, oksidovana purinska nukleozidna trifosfataza, (2'-dezoksi) ribonukleozidna 5'-trifosfatna pirofosfohidrolaza) je enzim sa sistematskim imenom 2-hidroksi-dATP difosfohidrolaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 2-hidroksi-dATP + H2O 2-hidroksi-dAMP + difosfat
Ovaj enzim hidrolizuje oksidovane purinske nukleozidne trifosfate.
- ↑ Sakumi, K., Furuichi, M., Tsuzuki, T., Kakuma, T., Kawabata, S., Maki, H. and Sekiguchi, M. (1993). „Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis”. J. Biol. Chem. 268: 23524-23530. PMID 8226881.
- ↑ Kakuma, T., Nishida, J., Tsuzuki, T. and Sekiguchi, M. (1995). „Mouse MTH1 protein with 8-oxo-7,8-dihydro-2′-deoxyguanosine 5′-triphosphatase activity that prevents transversion mutation. cDNA cloning and tissue distribution”. J. Biol. Chem. 270: 25942-25948. PMID 7592783.
- ↑ Fujikawa, K., Kamiya, H., Yakushiji, H., Fujii, Y., Nakabeppu, Y. and Kasai, H. (1999). „The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein”. J. Biol. Chem. 274: 18201-18205. PMID 10373420.
- ↑ Sakai, Y., Furuichi, M., Takahashi, M., Mishima, M., Iwai, S., Shirakawa, M. and Nakabeppu, Y. (2002). „A molecular basis for the selective recognition of 2-hydroxy-dATP and 8-oxo-dGTP by human MTH1”. J. Biol. Chem. 277: 8579-8587. PMID 11756418.
- ↑ Fujikawa, K., Kamiya, H., Yakushiji, H., Nakabeppu, Y. and Kasai, H. (2001). „Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP”. Nucleic Acids Res. 29: 449-454. PMID 11139615.
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