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X‐ray structure of linalool dehydratase/isomerase from Castellaniella defragrans reveals enzymatic alkene synthesis
Author(s) -
Weidenweber Sina,
Marmulla Robert,
Ermler Ulrich,
Harder Jens
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12165
Subject(s) - linalool , chemistry , dehydratase , monoterpene , geraniol , alkene , isomerase , biocatalysis , myrcene , stereochemistry , organic chemistry , terpene , enzyme , limonene , catalysis , reaction mechanism , chromatography , essential oil
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 β‐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 (α,α) 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.