NUDT5 hydrolyzes oxidized deoxyribonucleoside diphosphates with broad substrate specificity
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概要
- 論文の詳細を見る
The human NUDT5 protein catalyzes the hydrolysis of 8-hydroxy-dGDP. To examine its substrate specificity, four oxidized deoxyribonucleotides (2-hydroxy-dADP, 8-hydroxy-dADP, 5-formyl-dUDP, and 5-hydroxy-dCDP) were incubated with the NUDT5 protein. Interestingly, all of the nucleotides, except for 5-hydroxy-dCDP, were hydrolyzed with various efficiencies. The kinetic parameters indicated that 8-hydroxy-dADP was hydrolyzed as efficiently as 8-hydroxy-dGDP. The hydrolyzing activities for their triphosphate counterparts were quite weak. These results suggest that the NUDT5 protein eliminates various oxidized deoxyribonucleoside diphosphates from the nucleotide pool and prevents their toxic effects.
- Elsevier B.V.の論文
- 2009-10-02
著者
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原島 秀吉
北大院・薬学研究科
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Hori Mika
北海道大学 薬学研究科
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Hori Mika
北海道大学 薬学研究院
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Hori Mika
Hokkaido University Graduate School Of Pharmaceutical Sciences
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Shim Chang
Faculty Of Pharmaceutical Sciences University Of Tokyo : (present Address) College Of Pharmacy Seoul
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Kamiya Hiroyuki
産業医科大学産業生態科学研究所
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Murata-kamiya Naoko
Inst. Indust. Ecolog. Sci. Univ. Occup. Environ. Hith.
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Kaji Hiroshi
Inst. Indust. Ecolog. Sci. Univ. Occup. Environ. Hith.
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