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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
18
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pubmed:dateCreated |
1999-10-12
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pubmed:abstractText |
We previously identified the prpBCDE operon, which encodes catabolic functions required for propionate catabolism in Salmonella typhimurium. Results from (13)C-labeling experiments have identified the route of propionate breakdown and determined the biochemical role of each Prp enzyme in this pathway. The identification of catabolites accumulating in wild-type and mutant strains was consistent with propionate breakdown through the 2-methylcitric acid cycle. Our experiments demonstrate that the alpha-carbon of propionate is oxidized to yield pyruvate. The reactions are catalyzed by propionyl coenzyme A (propionyl-CoA) synthetase (PrpE), 2-methylcitrate synthase (PrpC), 2-methylcitrate dehydratase (probably PrpD), 2-methylisocitrate hydratase (probably PrpD), and 2-methylisocitrate lyase (PrpB). In support of this conclusion, the PrpC enzyme was purified to homogeneity and shown to have 2-methylcitrate synthase activity in vitro. (1)H nuclear magnetic resonance spectroscopy and negative-ion electrospray ionization mass spectrometry identified 2-methylcitrate as the product of the PrpC reaction. Although PrpC could use acetyl-CoA as a substrate to synthesize citrate, kinetic analysis demonstrated that propionyl-CoA is the preferred substrate.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-10348870,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-10411265,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-13058835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-14898026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-2697751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-2844305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-3039301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-3766971,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-4554901,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-4565618,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-4568531,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-4862045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-4869938,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-4956126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-5781279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-6093859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-8098211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-8655535,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-8969508,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-8998991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-9006051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-9278503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-9325432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-9579066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-9634230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10482501-9851993
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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 |
Sep
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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 |
181
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5615-23
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10482501-Carbon Isotopes,
pubmed-meshheading:10482501-Citrate (si)-Synthase,
pubmed-meshheading:10482501-Citrates,
pubmed-meshheading:10482501-Genotype,
pubmed-meshheading:10482501-Isocitrates,
pubmed-meshheading:10482501-Kinetics,
pubmed-meshheading:10482501-Magnetic Resonance Spectroscopy,
pubmed-meshheading:10482501-Mass Spectrometry,
pubmed-meshheading:10482501-Models, Chemical,
pubmed-meshheading:10482501-Operon,
pubmed-meshheading:10482501-Oxo-Acid-Lyases,
pubmed-meshheading:10482501-Propionic Acids,
pubmed-meshheading:10482501-Salmonella typhimurium
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pubmed:year |
1999
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pubmed:articleTitle |
Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric acid cycle.
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pubmed:affiliation |
Department of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin 53706-1567, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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