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J. Biol. Chem., Vol. 281, Issue 32, 22794-22798, August 11, 2006

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Three New Nudix Hydrolases from Escherichia coli^*

From the Department of Biology and The McCollum Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218

Three members of the Nudix (nucleoside diphosphate X) hydrolase superfamily have been cloned from Escherichia coli MG1655 and expressed. The proteins have been purified and identified as enzymes active on nucleoside diphosphate derivatives with the following specificities. Orf141 (yfaO) is a nucleoside triphosphatase preferring pyrimidine deoxynucleoside triphosphates. Orf153 (ymfB) is a nonspecific nucleoside tri- and diphosphatase and atypically releases inorganic orthophosphate from triphosphates instead of pyrophosphate. Orf191 (yffH) is a highly active GDP-mannose pyrophosphatase. All three enzymes require a divalent cation for activity and are optimally active at alkaline pH, characteristic of the Nudix hydrolase superfamily. The question of whether or not Orf1.9 (wcaH) is a bona fide member of the Nudix hydrolase superfamily is discussed.

Received for publication, April 10, 2006 , and in revised form, June 8, 2006.

^* This work was supported by National Institutes of Heath Grant GM18649. This is publication 1529 from the McCollum-Pratt Institute. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Present address: Dept. of Chemistry, Rochester Institute of Technology, Rochester, NY 14623-5603.

² To whom correspondence should be addressed: Dept. of Biology and the McCollum-Pratt Institute, The Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218. Tel.: 410-516-7316; Fax: 410-516-5213; E-mail: zoot{at}jhu.edu.

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