PMID:15533835

Citation	Hori, M, Fujikawa, K, Kasai, H, Harashima, H and Kamiya, H (2005) Dual hydrolysis of diphosphate and triphosphate derivatives of oxidized deoxyadenosine by Orf17 (NtpA), a MutT-type enzyme. DNA Repair (Amst.) 4:33-9
Abstract	To determine whether the Orf17 (NtpA) protein of Escherichia coli, a MutT-type enzyme, functions as a hydrolyzing enzyme for a damaged deoxyribonucleotide, we purified the recombinant Orf17 protein and incubated it with oxidized deoxyribonucleotides. Of the deoxyribonucleoside 5'-triphosphates tested, 8-hydroxy-2'-deoxyadenosine 5'-triphosphate was hydrolyzed by this protein. Unexpectedly, the Orf17 protein degraded 8-hydroxy-2'-deoxyadenosine 5'-diphosphate 2.3-fold more efficiently than the corresponding triphosphate. Thus, this protein is the first MutT-type enzyme that hydrolyzes both the triphosphate and diphosphate derivatives of a deoxyribonucleoside, with similar efficiencies. These results suggest that the Orf17 protein may be involved in the hydrolysis of oxidized dATP and dADP.
Links	PubMed Online version:10.1016/j.dnarep.2004.07.010
Keywords	Cloning, Molecular; DNA Primers; Deoxyadenosines/metabolism; Deoxyribonucleotides/metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Hydrolysis; Phosphoric Monoester Hydrolases/genetics; Phosphoric Monoester Hydrolases/metabolism; Pyrophosphatases; Sequence Analysis, DNA
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