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Journal of Bacteriology, November 2004, p. 7635-7644, Vol. 186, No. 22
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.22.7635-7644.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Evidence that a B₁₂-Adenosyl Transferase Is Encoded within the Ethanolamine Operon of Salmonella enterica

David E. Sheppard,¹ Joseph T. Penrod,² Thomas Bobik,^3, Eric Kofoid,² and John R. Roth^2*

Department of Biological Sciences, University of Delaware, Newark, Delaware,¹ Section of Microbiology, Division of Biological Sciences, University of California, Davis, Davis, California,² Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida³

Received 5 June 2004/ Accepted 11 August 2004

Adenosylcobalamin (Ado-B₁₂) is both the cofactor and inducer of ethanolamine ammonia lyase (EA-lyase), a catabolic enzyme for ethanolamine. De novo synthesis of Ado-B₁₂ by Salmonella enterica occurs only under anaerobic conditions. Therefore, aerobic growth on ethanolamine requires import of Ado-B₁₂ or a precursor (CN-B₁₂ or OH-B₁₂) that can be adenosylated internally. Several known enzymes adenosylate corrinoids. The CobA enzyme transfers adenosine from ATP to a biosynthetic intermediate in de novo B₁₂ synthesis and to imported CN-B₁₂, OH-B₁₂, or Cbi (a B₁₂ precursor). The PduO adenosyl transferase is encoded in an operon (pdu) for cobalamin-dependent propanediol degradation and is induced by propanediol. Evidence is presented here that a third transferase (EutT) is encoded within the operon for ethanolamine utilization (eut). Surprisingly, these three transferases share no apparent sequence similarity. CobA produces sufficient Ado-B₁₂ to initiate eut operon induction and to serve as a cofactor for EA-lyase when B₁₂ levels are high. Once the eut operon is induced, the EutT transferase supplies more Ado-B₁₂ during the period of high demand. Another protein encoded in the operon (EutA) protects EA-lyase from inhibition by CN-B₁₂ but does so without adenosylation of this corrinoid.

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* Corresponding author. Mailing address: Section of Microbiology, DBS, University of California, Davis, One Shields Ave., Davis, CA 95616. Phone: (530) 752-6679. Fax: (530) 752-7663. E-mail: jrroth{at}ucdavis.edu.

Present address: Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, IA 50011.

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Journal of Bacteriology, November 2004, p. 7635-7644, Vol. 186, No. 22
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.22.7635-7644.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

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