5HLR

Linalool dehydratase/isomerase: Ldi-apo

5HLR の概要

• エントリーDOI: 10.2210/pdb5hlr/pdb
• 分子名称: Linalool dehydratase/isomerase, 2-(2-METHOXYETHOXY)ETHANOL (3 entities in total)
• 機能のキーワード: linalool dehydratase/isomerase, alpha6 alpha6 barrel fold, anaerobic degradation, monoterpene, isomerase
• 由来する生物種: Castellaniella defragrans
• 細胞内の位置: Periplasm : E1XUJ2
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 209913.33

構造登録者

Weidenweber, S.,Marmulla, R.,Harder, J.,Ermler, U. (登録日: 2016-01-15, 公開日: 2016-04-27, 最終更新日: 2024-10-09)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.911 Å)