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

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.

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Weidenweber, S., Author
Marmulla, R.1, Author           
Ermler, U., Author
Harder, J.1, Author           
Affiliations:
1Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society, ou_2481695              

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 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.

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Language(s): eng - English
 Dates: 2016-05
 Publication Status: Issued
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Internal
 Identifiers: eDoc: 732750
ISI: 000375528800009
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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 590 (9) Sequence Number: 1 Start / End Page: 1375 - 1383 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501