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Geraniol and Geranial Dehydrogenases Induced in Anaerobic Monoterpene Degradation by Castellaniella defragrans

MPS-Authors
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Lueddeke,  F.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Wuelfing,  A.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Timke,  M.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Germer,  F.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Weber,  J.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Dikfidan,  A.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Rahnfeld,  T.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Meyerdierks,  A.
Department of Molecular Ecology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Harder,  J.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Lueddeke12.pdf
(Publisher version), 530KB

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Citation

Lueddeke, F., Wuelfing, A., Timke, M., Germer, F., Weber, J., Dikfidan, A., et al. (2012). Geraniol and Geranial Dehydrogenases Induced in Anaerobic Monoterpene Degradation by Castellaniella defragrans. Applied and Environmental Microbiology, 78(7), 2128-2136.


Cite as: http://hdl.handle.net/21.11116/0000-0001-C84D-8
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 (k cat/K m = 2.02 × 106 M−1 s−1), followed by geraniol (k cat/K m = 1.57 × 106 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.