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http://purl.uniprot.org/citations/22286981http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22286981http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22286981http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/22286981http://www.w3.org/2000/01/rdf-schema#comment"Castellaniella defragrans is a Betaproteobacterium capable of coupling the oxidation of monoterpenes with denitrification. Geraniol dehydrogenase (GeDH) activity was induced during growth with limonene in comparison to growth with acetate. The N-terminal sequence of the purified enzyme directed the cloning of the corresponding open reading frame (ORF), the first bacterial gene for a GeDH (geoA, for geraniol oxidation pathway). The C. defragrans geraniol dehydrogenase is a homodimeric enzyme that affiliates with the zinc-containing benzyl alcohol dehydrogenases in the superfamily of medium-chain-length dehydrogenases/reductases (MDR). The purified enzyme most efficiently catalyzes the oxidation of perillyl alcohol (k(cat)/K(m) = 2.02 × 10(6) M(-1) s(-1)), followed by geraniol (k(cat)/K(m) = 1.57 × 10(6) M(-1) s(-1)). Apparent K(m) values of <10 μM are consistent with an in vivo toxicity of geraniol above 5 μM. In the genetic vicinity of geoA is a putative aldehyde dehydrogenase that was named geoB and identified as a highly abundant protein during growth with phellandrene. Extracts of Escherichia coli expressing geoB demonstrated in vitro a geranial dehydrogenase (GaDH) activity. GaDH activity was independent of coenzyme A. The irreversible formation of geranic acid allows for a metabolic flux from β-myrcene via linalool, geraniol, and geranial to geranic acid."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.org/dc/terms/identifier"doi:10.1128/aem.07226-11"xsd:string
http://purl.uniprot.org/citations/22286981http://purl.org/dc/terms/identifier"doi:10.1128/aem.07226-11"xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Meyerdierks A."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Meyerdierks A."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Weber J."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Weber J."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Harder J."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Harder J."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Linder D."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Linder D."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Dikfidan A."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Dikfidan A."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Germer F."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Germer F."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Luddeke F."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Luddeke F."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Rahnfeld T."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Rahnfeld T."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Timke M."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Timke M."xsd:string
http://purl.uniprot.org/citations/22286981http://purl.uniprot.org/core/author"Wulfing A."xsd:string