Abstract:
:The human mutT homolog, hMTH1, suppresses spontaneous mutations by degrading the endogeneous mutagen, 8-hydroxy-dGTP. We previously reported the broad substrate specificity of hMTH1, which also degrades the oxidatively damaged purine nucleotides, 2-hydroxy-dATP, 8-hydroxy-dATP, 2-hydroxy-ATP, and 8-hydroxy-GTP, in addition to 8-hydroxy-dGTP. In this paper, we describe the hMTH1 activity for 8-chloro-dGTP, which could be formed in inflamed tissue by the reaction of dGTP with hypochlorous acid, a product of myeloperoxidase from activated human neutrophils. The hMTH1 protein was mixed with 1-20 microM of 8-chloro-dGTP and 8-hydroxy-dGTP, and the reaction products were quantified by anion-exchange HPLC to measure the pyrophosphatase reaction rate. The kinetic parameters revealed that 8-chloro-dGTP was degraded by hMTH1 with 50% efficiency as compared with that of 8-hydroxy-dGTP. This result suggests that 8-chloro-dGTP is an intrinsic substrate for hMTH1.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Fujikawa K,Yakushiji H,Nakabeppu Y,Suzuki T,Masuda M,Ohshima H,Kasai Hdoi
10.1016/s0014-5793(02)02240-8keywords:
subject
Has Abstractpub_date
2002-02-13 00:00:00pages
149-51issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302022408journal_volume
512pub_type
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