Nucleotide triphosphate diphosphatase NUDT15 (EC 3.6.1.9) (MutT homolog 2) (MTH2) (Nucleoside diphosphate-linked moiety X motif 15) (Nudix motif 15) (Nucleoside diphosphate-linked to another moiety X hydrolase 15) (Nudix hydrolase 15)
1_MTASA 6_ QPRGR 11_ RPGVG 16_ VGVVV 21_ TSCKH 26_ PRCVL 31_ LGKRK 36_ GSVGA 41_ GSFQL 46_ PGGHL 51_ EFGET 56_ WEECA 61_ QRETW 66_ EEAAL 71_ HLKNV 76_ HFASV 81_ VNSFI 86_ EKENY 91_ HYVTI 96_ LMKGE 101_ VDVTH 106_ DSEPK 111_ NVEPE 116_ KNESW 121_ EWVPW 126_ EELPP 131_ LDQLF 136_ WGLRC 141_ LKEQG 146_ YDPFK 151_ EDLNH 156_LVGYK
1: May catalyze the hydrolysis of nucleoside triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP and the prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP (PubMed:26238318). Could also catalyze the hydrolysis of some nucleoside diphosphate derivatives (PubMed:22556419, PubMed:26238318). Hydrolyzes oxidized nucleosides triphosphates like 8-oxo-dGTP in vitro, but the specificity and efficiency towards these substrates are low. Therefore, the potential in vivo sanitizing role of this enzyme, that would consist in removing oxidatively damaged forms of nucleosides to prevent their incorporation into DNA, is unclear (PubMed:22556419, PubMed:26238318). Through the hydrolysis of thioguanosine triphosphates may participate in the catabolism of thiopurine drugs (PubMed:25108385, PubMed:26238318). May also have a role in DNA synthesis and cell cycle progression by stabilizing PCNA (PubMed:19419956). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity)