5G1U

Linalool Dehydratase Isomerase in complex with Geraniol

5G1U の概要

• エントリーDOI: 10.2210/pdb5g1u/pdb
• 関連するPDBエントリー: 5G1V 5G1W
• 分子名称: LINALOOL DEHYDRATASE/ISOMERASE, Geraniol (3 entities in total)
• 機能のキーワード: hydratase, isomerase, terpene, lyase
• 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: 213084.55

構造登録者

Chambers, S.,Hau, A.,Man, H.,Omar, M.,Turkenburg, J.P.,Grogan, G. (登録日: 2016-03-30, 公開日: 2017-01-11, 最終更新日: 2024-10-09)

主引用文献

Nestl, B.M.,Geinitz, C.,Popa, S.,Rizek, S.,Haselbeck, R.J.,Stephen, R.,Noble, M.A.,Fischer, M.P.,Ralph, E.C.,Hau, H.T.,Man, H.,Omar, M.,Turkenburg, J.P.,van Dien, S.,Culler, S.J.,Grogan, G.,Hauer, B.
Structural and functional insights into asymmetric enzymatic dehydration of alkenols.
Nat. Chem. Biol., 13:275-281, 2017

PubMed Abstract: The asymmetric dehydration of alcohols is an important process for the direct synthesis of alkenes. We report the structure and substrate specificity of the bifunctional linalool dehydratase isomerase (LinD) from the bacterium Castellaniella defragrans that catalyzes in nature the hydration of β-myrcene to linalool and the subsequent isomerization to geraniol. Enzymatic kinetic resolutions of truncated and elongated aromatic and aliphatic tertiary alcohols (C5-C15) that contain a specific signature motif demonstrate the broad substrate specificity of LinD. The three-dimensional structure of LinD from Castellaniella defragrans revealed a pentamer with active sites at the protomer interfaces. Furthermore, the structure of LinD in complex with the product geraniol provides initial mechanistic insights into this bifunctional enzyme. Site-directed mutagenesis confirmed active site amino acid residues essential for its dehydration and isomerization activity. These structural and mechanistic insights facilitate the development of hydrating catalysts, enriching the toolbox for novel bond-forming biocatalysis.

PubMed: 28068311
DOI: 10.1038/nchembio.2271

実験手法

X-RAY DIFFRACTION (2.57 Å)