5G1V

Linalool Dehydratase Isomerase: Selenomethionine Derivative

Summary for 5G1V

• Entry DOI: 10.2210/pdb5g1v/pdb
• Related: 5G1U 5G1W
• Descriptor: LINALOOL DEHYDRATASE ISOMERASE (2 entities in total)
• Functional Keywords: hydratase, linalool, terpene, lyase, isomerase
• Biological source: CASTELLANIELLA DEFRAGRANS
• Cellular location: Periplasm : E1XUJ2
• Total number of polymer chains: 5
• Total formula weight: 212313.30

Authors

Chambers, S.,Hau, A.,Man, H.,Omar, M.,Turkenburg, J.P.,Grogan, G. (deposition date: 2016-03-30, release date: 2017-01-11, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.68 Å)