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Originally published In Press as doi:10.1074/jbc.M004100200 on October 26, 2000

J. Biol. Chem., Vol. 276, Issue 8, 5421-5426, February 23, 2001
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Orf135 from Escherichia coli Is a Nudix Hydrolase Specific for CTP, dCTP, and 5-Methyl-dCTP*

Suzanne F. O'HandleyDagger , Christopher A. Dunn, and Maurice J. Bessman

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

Orf135 from Escherichia coli is a new member of the Nudix (nucleoside diphosphate linked to some other moiety, x) hydrolase family of enzymes with substrate specificity for CTP, dCTP, and 5-methyl-dCTP. The gene has been cloned for overexpression, and the protein has been overproduced, purified, and characterized. Orf135 is most active on 5-methyl-dCTP (kcat/Km = 301,000 M-1 s-1), followed by CTP (kcat/Km = 47,000 M-1 s-1) and dCTP (kcat/Km = 18,000 M-1 s-1). Unlike other nucleoside triphosphate pyrophophohydrolases of the Nudix hydrolase family discovered thus far, Orf135 is highly specific for pyrimidine (deoxy)nucleoside triphosphates. Like other Nudix hydrolases, the enzyme cleaves its substrates to produce a nucleoside monophosphate and inorganic pyrophosphate, has an alkaline pH optimum, and requires a divalent metal cation for catalysis, with magnesium yielding optimal activity. Because of the nature of its substrate specificity, Orf135 may play a role in pyrimidine biosynthesis, lipid biosynthesis, and in controlling levels of 5-methyl-dCTP in the cell.

* This work was supported by National Institutes of Health Grant GM 18649. This is publication 1523 from the McCollum-Pratt Institute.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Present address: Dept. of Chemistry, University of Richmond, Richmond, VA 23173. To whom correspondence should be addressed. Tel.: 804-289-8245; Fax: 804-287-1897; E-mail: sohandle@richmond.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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