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Article

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

Journal of bacteriology - 1 Nov 2004

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

Abstract excerpt

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...

Topics

Alkyl and Aryl Transferases
Bacterial Proteins
Cobamides
Culture Media
Ethanolamine
Ethanolamine Ammonia-Lyase
Gene Expression Regulation, Bacterial
Gene Expression Regulation, Enzymologic
Mutation
Operon

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Salmonella typhimurium

Source

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Identifiers

PMID: 15516577
DOI: 10.1128/JB.186.22.7635-7644.2004
PMCID: PMC524904

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Evidence that a B12-adenosyl transferase is encoded within the ethanolamine operon of Salmonella enterica.PMID 15516577Read ↗

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Minimal functions and physiological conditions required for growth of salmonella enterica on ethanolamine in the absence of the metabolosome.Semantic proximity Read ↗

The eutT gene of Salmonella enterica Encodes an oxygen-labile, metal-containing ATP:corrinoid adenosyltransferase enzyme.Semantic proximity Read ↗

One pathway can incorporate either adenine or dimethylbenzimidazole as an alpha-axial ligand of B12 cofactors in Salmonella enterica.Semantic proximity Read ↗

A rationale for autoinduction of a transcriptional activator: ethanolamine ammonia-lyase (EutBC) and the operon activator (EutR) compete for adenosyl-cobalamin in Salmonella typhimurium.Semantic proximity Read ↗

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