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J Biol Chem, Vol. 274, Issue 26, 18201-18205, June 25, 1999
From the The possibility that Escherichia coli
MutT and human MTH1 (hMTH1) hydrolyze oxidized DNA precursors other
than 8-hydroxy-dGTP (8-OH-dGTP) was investigated. We report here that
hMTH1 hydrolyzed 2-hydroxy-dATP (2-OH-dATP) and 8-hydroxy-dATP
(8-OH-dATP), oxidized forms of dATP, but not
(R)-8,5'-cyclo-dATP, 5-hydroxy-dCTP, and 5-formyl-dUTP. The
kinetic parameters indicated that 2-OH-dATP was hydrolyzed more
efficiently and with higher affinity than 8-OH-dGTP. 8-OH-dATP was
hydrolyzed as efficiently as 8-OH-dGTP. The preferential hydrolysis of
2-OH-dATP over 8-OH-dGTP was observed at all of the pH values tested
(pH 7.2 to pH 8.8). In particular, a 5-fold difference in the
hydrolysis efficiencies for 2-OH-dATP over 8-OH-dGTP was found at pH
7.2. However, E. coli MutT had no hydrolysis activity for
either 2-OH-dATP or 8-OH-dATP. Thus, E. coli MutT is an
imperfect counterpart for hMTH1. Furthermore, we found that
2-hydroxy-dADP and 8-hydroxy-dGDP competitively inhibited both the
2-OH-dATP hydrolase and 8-OH-dGTP hydrolase activities of hMTH1. The
inhibitory effects of 2-hydroxy-dADP were 3-fold stronger than those of
8-hydroxy-dGDP. These results suggest that the three damaged
nucleotides share the same recognition site of hMTH1 and that it is a
more important sanitization enzyme than expected thus far.
The Oxidized Forms of dATP Are Substrates for the Human MutT
Homologue, the hMTH1 Protein
,,
Department of Environmental Oncology,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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