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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
22
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pubmed:dateCreated |
2004-11-1
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pubmed:abstractText |
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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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-10383983,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-10464203,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-10498708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-11160088,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-11274105,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-11844753,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-1328159,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-14996820,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-1550360,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-2403541,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-2656649,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-2687248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-3045078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-33657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-342507,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-4308003,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-4544750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-4874308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-5787789,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-6099322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-6376471,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-784902,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-8113167,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-8905078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-9294441,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15516577-9920879
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
186
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7635-44
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15516577-Alkyl and Aryl Transferases,
pubmed-meshheading:15516577-Bacterial Proteins,
pubmed-meshheading:15516577-Cobamides,
pubmed-meshheading:15516577-Culture Media,
pubmed-meshheading:15516577-Ethanolamine,
pubmed-meshheading:15516577-Ethanolamine Ammonia-Lyase,
pubmed-meshheading:15516577-Gene Expression Regulation, Bacterial,
pubmed-meshheading:15516577-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:15516577-Mutation,
pubmed-meshheading:15516577-Operon,
pubmed-meshheading:15516577-Salmonella typhimurium
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pubmed:year |
2004
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pubmed:articleTitle |
Evidence that a B12-adenosyl transferase is encoded within the ethanolamine operon of Salmonella enterica.
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pubmed:affiliation |
Department of Biological Sciences, University of Delaware, Newark, Delaware, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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