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J Biol Chem. 2006 Aug 11;281(32):22794-8. Epub 2006 Jun 9.

Three new Nudix hydrolases from Escherichia coli.

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  • 1Department of Biology and The McCollum Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218, USA.

Abstract

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.

PMID:
16766526
DOI:
10.1074/jbc.M603407200
[PubMed - indexed for MEDLINE]
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