Source:http://linkedlifedata.com/resource/pubmed/id/18364348
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
23
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pubmed:dateCreated |
2008-6-2
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pubmed:abstractText |
Although the D-glucarate degradation pathway is well characterized in Escherichia coli, genetic and biochemical information concerning the alternative pathway proposed in Pseudomonas species and Bacillus subtilis remains incomplete. Acinetobacter baylyi ADP1 is a Gram-negative soil bacterium possessing the alternative pathway and able to grow using D-glucarate as the only carbon source. Based on the annotation of its sequenced genome (1), we have constructed a complete collection of singlegene deletion mutants (2). High throughput profiling for growth on a minimal medium containing D-glucarate as the only carbon source for approximately 2450 mutants led to the identification of the genes involved in D-glucarate degradation. Protein purification after recombinant production in E. coli allowed us to reconstitute the enzymatic pathway in vitro. We describe here the kinetic characterization of D-glucarate dehydratase, d-5-keto-4-deoxyglucarate dehydratase, and of cooperative alpha-ketoglutarate semialdehyde dehydrogenase. Transcription and expression analyses of the genes involved in D-glucarate metabolism within a single organism made it possible to access information regarding the regulation of this pathway for the first time.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutarates,
http://linkedlifedata.com/resource/pubmed/chemical/Hydro-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/glucarate dehydratase
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:AghaieAsadollahA,
pubmed-author:Besnard-GonnetMarielleM,
pubmed-author:GyapayGaborG,
pubmed-author:KreimeyerAnnettA,
pubmed-author:LechaplaisChristopheC,
pubmed-author:MuseletDelphineD,
pubmed-author:PerretAlainA,
pubmed-author:SalanoubatMarcelM,
pubmed-author:SirvenPeggyP,
pubmed-author:TricotSabineS,
pubmed-author:de BerardinisVéroniqueV
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
283
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15638-46
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pubmed:meshHeading |
pubmed-meshheading:18364348-Acinetobacter,
pubmed-meshheading:18364348-Bacterial Proteins,
pubmed-meshheading:18364348-Gene Deletion,
pubmed-meshheading:18364348-Gene Expression Regulation, Bacterial,
pubmed-meshheading:18364348-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:18364348-Genome, Bacterial,
pubmed-meshheading:18364348-Glutarates,
pubmed-meshheading:18364348-Hydro-Lyases,
pubmed-meshheading:18364348-Recombinant Proteins,
pubmed-meshheading:18364348-Transcription, Genetic
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pubmed:year |
2008
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pubmed:articleTitle |
New insights into the alternative D-glucarate degradation pathway.
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pubmed:affiliation |
CNRS-UMR 8030, Genoscope-Commissariat à l'Energie Atomique, 2 Rue Gaston Crémieux, Evry 91057, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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