5HLR

Linalool dehydratase/isomerase: Ldi-apo

Summary for 5HLR

• Entry DOI: 10.2210/pdb5hlr/pdb
• Descriptor: Linalool dehydratase/isomerase, 2-(2-METHOXYETHOXY)ETHANOL (3 entities in total)
• Functional Keywords: linalool dehydratase/isomerase, alpha6 alpha6 barrel fold, anaerobic degradation, monoterpene, isomerase
• Biological source: Castellaniella defragrans
• Cellular location: Periplasm : E1XUJ2
• Total number of polymer chains: 5
• Total formula weight: 209913.33

Authors

Weidenweber, S.,Marmulla, R.,Harder, J.,Ermler, U. (deposition date: 2016-01-15, release date: 2016-04-27, Last modification date: 2024-10-09)

Primary citation

Weidenweber, S.,Marmulla, R.,Ermler, U.,Harder, J.
X-ray structure of linalool dehydratase/isomerase from Castellaniella defragrans reveals enzymatic alkene synthesis.
Febs Lett., 590:1375-1383, 2016

PubMed 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.

PubMed: 27062179
DOI: 10.1002/1873-3468.12165

Experimental method

X-RAY DIFFRACTION (1.911 Å)