Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP
Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP
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DOI:
10.1093/nar/29.2.449
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发表时间:
2001-01-15
影响因子:
14.9
通讯作者:
Kasai, H
中科院分区:
文献类型:
--
作者:
Fujikawa, K;Kamiya, H;Kasai, H
The human nucleotide pool sanitization enzyme, MTH1, hydrolyzes 2-hydroxy-dATP and 8-hydroxy-dATP in addition to 8-hydroxy-dGTP. We report here that human MTH1 is highly specific for a-hydroxy-ATP, among the cognate ribonucleoside triphosphates. The pyrophosphatase activities for 8-hydroxy-GTP, 2-hydroxy-ATP and 8-hydroxy-ATP were measured by high-performance liquid chromatography, The kinetic parameters thus obtained indicate that the catalytic efficiencies of MTH1 are in the order of 2-hydroxy-dATP > 2-hydroxy-ATP > 8-hydroxy-GTP > 8-hydroxy-dATP >> dGTP > 8-hydroxy-GTP > 8-hydroxy-ATP. Notably, MTH1 had the highest affinity for P-hydroxy-ATP among the known substrates, ATP is involved in energy metabolism and signal transduction, and is a precursor in RNA synthesis. We suggest that the 2-hydroxy-ATP hydrolyzing activity of MTH1 might prevent the perturbation of these ATP-related pathways by the oxidized ATP.