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Originally published In Press as doi:10.1074/jbc.M203893200 on June 21, 2002

J. Biol. Chem., Vol. 277, Issue 36, 33127-33131, September 6, 2002
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The ATP:Co(I)rrinoid Adenosyltransferase (CobA) Enzyme of Salmonella enterica Requires the 2'-OH Group of ATP for Function and Yields Inorganic Triphosphate as Its Reaction Byproduct*

Maris V. FonsecaDagger §, Nicole R. BuanDagger , Alexander R. HorswillDagger ||, Ivan Rayment**Dagger Dagger , and Jorge C. Escalante-SemerenaDagger §§

From the Departments of Dagger  Bacteriology and ** Biochemistry, University of Wisconsin, Madison, Wisconsin 53706

The specificity of the ATP:corrinoid adenosyltransferase (CobA) enzyme of Salmonella enterica serovar Typhimurium LT2 for its nucleotide substrate was tested using ATP analogs and alternative nucleotide donors. The enzyme showed broad specificity for the nucleotide base and required the 2'-OH group of the ribosyl moiety of ATP for activity. 31P NMR spectroscopy was used to identify inorganic triphosphate (PPPi) as the byproduct of the reaction catalyzed by the CobA enzyme. Cleavage of triphosphate into pyrophosphate and orthophosphate did not occur, indicating that triphosphate cleavage was not required for release of the adenosylcorrinoid product. Triphosphate was a strong inhibitor of the reaction, with 85% of CobA activity lost when the ATP/PPPi ratio present in the reaction mixture was 1:2.5.

* This work was supported in part by National Institutes of Health Grant GM40313 and by a Dupont Aid-To-Education grant (to J. C. E.-S.) and by National Institutes of Health Grant GM58281 (to I. R.).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.

§ Recipient of a National Institutes of Health MARC Fellowship GM17528 and an Advanced Opportunity Fellowship (AOF) from The Graduate School of the University of Wisconsin-Madison. Present address: Infectious Diseases Research, Eli Lilly and Co., Lilly Corporate Center DC 1543, Indianapolis, IN 46285.

A Howard Hughes Medical Institute predoctoral fellow.

|| Supported by National Institutes of Health Biotechnology Grant GM08349 and a National Science Foundation predoctoral fellowship. Present address: Dept. of Chemistry, Pennsylvania State University, University Park, PA 16802.

Dagger Dagger To whom correspondence may be addressed: Dept. of Biochemistry, 433 Babcock Dr., Madison, WI 53706. E-mail: ivan_rayment@biochem.wisc.edu.

§§ To whom correspondence may be addressed: Dept. of Bacteriology, 1550 Linden Dr., Madison, WI 53706. E-mail: escalante@bact.wisc.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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