EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
3.6.1.55 | 756066 |
Crystal structure and substrate specificity of the 8-oxo-dGTP hydrolase NUDT1 from Arabidopsis thaliana |
Biochemistry |
58 |
887-899 |
2019 |
Arabidopsis thaliana |
30614695 |
3.6.1.55 | 756449 |
Inhibitory effect of 8-halogenated 7-deaza-2-deoxyguanosine triphosphates on human 8-oxo-2'-deoxyguanosine triphosphatase, hMTH1, activities |
ChemBioChem |
17 |
566-569 |
2016 |
Homo sapiens |
26879218 |
3.6.1.55 | 756182 |
Insights into the substrate specificity of the MutT pyrophosphohydrolase using structural analogues of 8-oxo-2'-deoxyguanosine nucleotide |
Bioorg. Med. Chem. Lett. |
26 |
2014-2017 |
2016 |
Escherichia coli |
26965860 |
3.6.1.55 | 755779 |
Investigation of MTH1 activity via mismatch-based DNA chain elongation |
Anal. Chim. Acta |
905 |
66-71 |
2016 |
Homo sapiens |
26755138 |
3.6.1.55 | 757513 |
Structural insights into the specificity and catalytic mechanism of mycobacterial nucleotide pool sanitizing enzyme MutT2 |
J. Struct. Biol. |
204 |
449-456 |
2018 |
Mycolicibacterium smegmatis |
30312643 |
3.6.1.55 | 757513 |
Structural insights into the specificity and catalytic mechanism of mycobacterial nucleotide pool sanitizing enzyme MutT2 |
J. Struct. Biol. |
204 |
449-456 |
2018 |
Mycolicibacterium smegmatis mc(2)155 |
30312643 |
3.6.1.55 | 715460 |
A molecular basis for the selective recognition of 2-hydroxy-dATP and 8-oxo-dGTP by human MTH1 |
J. Biol. Chem. |
277 |
8579-8587 |
2002 |
Escherichia coli |
11756418 |
3.6.1.55 | 715113 |
CiMutT, an asidian MutT homologue, has a 7, 8-dihydro-8-oxo-dGTP pyrophosphohydrolase activity responsible for sanitization of oxidized nucleotides in Ciona intestinalis |
Genes Genet. Syst. |
85 |
287-295 |
2010 |
Ciona intestinalis |
21178309 |
3.6.1.55 | 716917 |
Counteraction by MutT protein of transcriptional errors caused by oxidative damage |
Science |
278 |
128-130 |
1997 |
Escherichia coli |
9311918 |
3.6.1.55 | 716070 |
Enhanced resolution of molecular recognition to distinguish structurally similar molecules by different conformational responses of a protein upon ligand binding |
J. Struct. Biol. |
173 |
20-28 |
2011 |
Escherichia coli |
20888916 |