Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10823704 | DNA Repair | 2005 | 7 Pages |
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 5â²-triphosphates tested, 8-hydroxy-2â²-deoxyadenosine 5â²-triphosphate was hydrolyzed by this protein. Unexpectedly, the Orf17 protein degraded 8-hydroxy-2â²-deoxyadenosine 5â²-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.
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Authors
Mika Hori, Katsuyoshi Fujikawa, Hiroshi Kasai, Hideyoshi Harashima, Hiroyuki Kamiya,