PDBsum entry 5hss

Lyase

PDB id: 5hss

Contents

Protein chains

366 a.a.

Ligands

PG0 ×5

64Z ×3

650 ×2

Waters ×121

PDB id:

5hss

Name:

Lyase

Title:

Linalool dehydratase/isomerase: ldi with monoterpene substrate

Structure:

Linalool dehydratase/isomerase. Chain: a, b, c, d, e. Synonym: geraniol isomerase,linalool dehydratase-isomerase,myrcene hydratase. Engineered: yes

Source:

Castellaniella defragrans. Organism_taxid: 75697. Gene: ldi. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008

Resolution:

2.50Å R-factor: 0.181 R-free: 0.223

Authors:

S.Weidenweber,R.Marmulla,J.Harder,U.Ermler

Key ref:

S.Weidenweber et al. (2016). X-ray structure of linalool dehydratase/isomerase from Castellaniella defragrans reveals enzymatic alkene synthesis. Febs Lett, 590, 1375-1383. PubMed id: 27062179 DOI: 10.1002/1873-3468.12165

Date:

26-Jan-16 Release date: 27-Apr-16

Protein chains

E1XUJ2  (LDI_CASD6) -  Linalool dehydratase/isomerase from Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen)

Seq: 397 a.a.

Struc: 366 a.a.

Enzyme reactions

• Enzyme class 1: E.C.4.2.1.127 - linalool dehydratase.
• Reaction: (S)-linalool = beta-myrcene + H2O

(S)-linalool = beta-myrcene (Bound ligand (Het Group name = 64Z) matches with 90.91% similarity) + H2O

• Enzyme class 2: E.C.5.4.4.4 - geraniol isomerase.
• Reaction: (2E)-geraniol = (S)-linalool

Geraniol (Bound ligand (Het Group name = 64Z) corresponds exactly) = linalool

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1002/1873-3468.12165

Febs Lett 590:1375-1383 (2016)

PubMed id: 27062179

X-ray structure of linalool dehydratase/isomerase from Castellaniella defragrans reveals enzymatic alkene synthesis.

S.Weidenweber, R.Marmulla, U.Ermler, J.Harder.

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.