ArticleFish physiology and biochemistry2026
Enzymatic catabolism of the mutagenic DNA precursor, 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate (8-oxo-dGTP), in rainbow trout liver.
Article in Fish physiology and biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
We characterized the catabolic pathway of 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate (8-oxo-dGTP) in the liver of rainbow trout (a representative of lower vertebrates) and determined the specific levels of all involved enzymatic activities. We analyzed the time-course kinetics of enzymatic hydrolysis of 40 µM 8-oxo-dGTP, 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-diphosphate (8-oxo-dGDP), and 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-monophosphate (8-oxo-dGMP) by an extract of rainbow trout liver at pH 8.5 and 5.5. Four different enzymatic activities were found to participate in decomposition of 8-oxo-dGTP to a final product 8-oxo-7,8-dihydro-2'-deoxyguanosine (8-oxo-dG), i.e., 8-oxo-dGTP pyrophosphohydrolase (specific activity at pH 8.5 107 U/mg protein, inactive at pH 5.5), 8-oxo-dGTP monophosphohydrolase (105 U/mg protein at pH 8.5, 181 U/mg protein at pH 5.5), 8-oxo-dGDP monophosphohydrolase (56 U/mg protein at pH 8.5, 188 U/mg protein at pH 5.5), and 8-oxo-dGMP phosphohydrolase (178 U/mg protein at pH 8.5, 485 U/mg protein at pH 5.5). At pH 8.5, all four enzymatic activities appeared to be dependent on magnesium ions (5 mM), as they were inhibited by 12.5 mM divalent metal ion chelator, ethylenediaminetetraacetic acid (EDTA). However, EDTA did not inhibit any of the three enzymatic activities detected at pH 5.5. There are two possible explanations for this phenomenon. The chelating power of EDTA in an acidic environment may be too low to remove Mg
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