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James M Bobbitt - One of the best experts on this subject based on the ideXlab platform.

Nabyl Merbouh - One of the best experts on this subject based on the ideXlab platform.

Leon J Tilley - One of the best experts on this subject based on the ideXlab platform.

Jens Harder - One of the best experts on this subject based on the ideXlab platform.

  • the anaerobic linalool metabolism in thauera linaloolentis 47 lol
    BMC Microbiology, 2016
    Co-Authors: Robert Marmulla, Edinson Puentes Cala, Stephanie Markert, Thomas Schweder, Jens Harder
    Abstract:

    Background The betaproteobacterium Thauera linaloolentis 47LolT was isolated on the tertiary monoterpene alcohol (R,S)-linalool as sole carbon and energy source under denitrifying conditions. Growth experiments indicated the formation of Geraniol and geranial. Thus, a 3,1-hydroxyl-Δ1-Δ2-mutase (linalool isomerase) activity may initiate the degradation, followed by enzymes of the acyclic terpene utilization (Atu) and leucine/isovalerate utilization (Liu) pathways that were extensively studied in Pseudomonas spp. growing on citronellol or Geraniol.

  • physiology of deletion mutants in the anaerobic β myrcene degradation pathway in castellaniella defragrans
    BMC Microbiology, 2012
    Co-Authors: Frauke Luddeke, Aytac Dikfidan, Jens Harder
    Abstract:

    Background Monoterpenes present a large and versatile group of unsaturated hydrocarbons of plant origin with widespread use in the fragrance as well as food industry. The anaerobic β-myrcene degradation pathway in Castellaniella defragrans strain 65Phen differs from well known aerobic, monooxygenase-containing pathways. The initial enzyme linalool dehydratase-isomerase ldi/LDI catalyzes the hydration of β-myrcene to (S)-(+)-linalool and its isomerization to Geraniol. A high-affinity Geraniol dehydrogenase geoA/GeDH and a geranial dehydrogenase geoB/GaDH contribute to the formation of geranic acid. A genetic system was for the first time applied for the betaproteobacterium to prove in vivo the relevance of the linalool dehydratase-isomerase and the Geraniol dehydrogenase. In-frame deletion cassettes were introduced by conjugation and two homologous recombination events.

  • Geraniol and geranial dehydrogenases induced in anaerobic monoterpene degradation by castellaniella defragrans
    Applied and Environmental Microbiology, 2012
    Co-Authors: Frauke Luddeke, Annika Wulfing, Markus Timke, Frauke Germer, Johanna Weber, Aytac Dikfidan, Tobias Rahnfeld, Dietmar Linder, Anke Meyerdierks, Jens Harder
    Abstract:

    ABSTRACT 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 ge raniol o xidation 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 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.

  • Geraniol and geranial dehydrogenases induced in anaerobic monoterpene degradation by castellaniella defragrans
    Applied and Environmental Microbiology, 2012
    Co-Authors: Frauke Luddeke, Annika Wulfing, Markus Timke, Frauke Germer, Johanna Weber, Aytac Dikfidan, Tobias Rahnfeld, Dietmar Linder, Anke Meyerdierks, Jens Harder
    Abstract:

    ABSTRACT 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 (kcat/Km = 2.02 × 106 M−1 s−1), followed by Geraniol (kcat/Km = 1.57 × 106 M−1 s−1). Apparent Km values of

Stephanie A Murray - One of the best experts on this subject based on the ideXlab platform.