X‐ray structure of linalool dehydratase/isomerase from Castellaniella defragrans reveals enzymatic alkene synthesis. Issue 9 (18th April 2016)

• Record Type: Journal Article
• Authors: Weidenweber, Sina; Marmulla, Robert; Ermler, Ulrich; Harder, Jens
• Is Part Of: FEBS letters. Volume 590:Issue 9(2016)
• Page Start: 1375
• Page End: 1383
• Publication Date: 2016-04-18
• Subjects: (α, α)6 barrel -- acid/base catalysis -- isoprenoids -- linalool dehydratase/isomerase -- monoterpene degradation; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12165
• Languages: English
• ISSNs: 0014-5793

Abstract

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 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. Abstract :