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X-ray structure of linalool dehydratase/isomerase from Castellaniella defragrans reveals enzymatic alkene synthesis

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Marmulla,  R.
Department of Microbiology, 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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Citation

Weidenweber, S., Marmulla, R., Ermler, U., & Harder, J. (2016). X-ray structure of linalool dehydratase/isomerase from Castellaniella defragrans reveals enzymatic alkene synthesis. FEBS Letters, 590(9): 1, pp. 1375-1383.


Cite as: https://hdl.handle.net/21.11116/0000-0001-C2EC-A
Abstract
Linalool dehydratase/isomerase (Ldi), an enzyme of terpene degradation in Castellaniella defragrans, isomerizes the primary monoterpene alcohol geraniol into the tertiary alcohol (S)-linalool and dehydrates (S)-linalool to the alkene b-myrcene. Here we report on the crystal structures of Ldi with and without terpene substrates, revealing a cofactor-free homopentameric enzyme. The substrates were embedded inside a hydrophobic channel between two monomers of the (alpha,alpha)(6) barrel fold class and flanked by three clusters of polar residues involved in acid-base catalysis. The detailed view into the active site will guide future biotechnological applications of Ldi, in particular, for industrial butadiene and isoprene production from renewable sources.