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Journal of Bacteriology, December 2004, p. 8380-8384, Vol. 186, No. 24
0021-9193/04/$08.00+0 DOI: 10.1128/JB.186.24.8380-8384.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Department of Biology and the McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, Maryland
Received 9 July 2004/ Accepted 10 September 2004
Gene ytkD of Bacillus subtilis, a member of the Nudix hydrolase superfamily, has been cloned and expressed in Escherichia coli. The purified protein has been characterized as a nucleoside triphosphatase active on all of the canonical ribo- and deoxyribonucleoside triphosphates. Whereas all other nucleoside triphosphatase members of the superfamily release inorganic pyrophosphate and the cognate nucleoside monophosphate, YtkD hydrolyses nucleoside triphosphates in a stepwise fashion through the diphosphate to the monophosphate, releasing two molecules of inorganic orthophosphate. Contrary to a previous report, our enzymological and genetic studies indicate that ytkD is not an orthologue of E. coli mutT.
Publication 1528 of the McCollum-Pratt Institute.
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