Evidence that a B12-adenosyl transferase is encoded within the ethanolamine operon of Salmonella enterica

David E. Sheppard, Joseph T. Penrod, Thomas Bobik, Eric Kofoid, John R. Roth

Research output: Contribution to journalArticlepeer-review

44 Scopus citations


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-B 12, 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.

Original languageEnglish (US)
Pages (from-to)7635-7644
Number of pages10
JournalJournal of Bacteriology
Issue number22
StatePublished - Nov 2004

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology


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