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PDBsum entry 5hss
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References listed in PDB file
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Key reference
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Title
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X-Ray structure of linalool dehydratase/isomerase from castellaniella defragrans reveals enzymatic alkene synthesis.
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Authors
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S.Weidenweber,
R.Marmulla,
U.Ermler,
J.Harder.
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Ref.
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Febs Lett, 2016,
590,
1375-1383.
[DOI no: ]
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PubMed id
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Abstract
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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.
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