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Literature summary for 4.2.1.127 extracted from

  • Weidenweber, S.; Marmulla, R.; Ermler, U.; Harder, J.
    X-ray structure of linalool dehydratase/isomerase from Castellaniella defragrans reveals enzymatic alkene synthesis (2016), FEBS Lett., 590, 1375-1383 .
    View publication on PubMed
Search for more literature for 4.2.1.127

Activating Compound

Activating Compound Comment Organism Structure
DTT a reductant is required for activity Castellaniella defragrans
additional information dehydratase and isomerase activities of the bifunctional Ldi are only detectable in the presence of a reductant (dithiothreitol) and in the absence of O2 Castellaniella defragrans

Application

Application Comment Organism
biotechnology possible biotechnological applications of Ldi, in particular, are industrial butadiene and isoprene production from renewable sources Castellaniella defragrans
synthesis the dehydration reaction of Ldi or genetically engineered variants thereof can be used for the transformation of smaller substrate molecules into butadiene and isoprene Castellaniella defragrans

Cloned(Commentary)

Cloned (Comment) Organism
gene ldi, recombinant expression in Escherichia coli strain BL21(DE3) Castellaniella defragrans

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme Ldi, free or in complex with thiomersal and/or linalool, sitting and hanging drop vapor diffusion method, 4 different crystallization methods, using PEG 550 MME, DTT, and bicine buffer, pH 9.0, overview. X-ray diffraction structure determination and analysis at 1.9 A resolution, single isomorphous replacement anomalous scattering method using thimerosal as heavy metal compound Castellaniella defragrans

Inhibitors

Inhibitors Comment Organism Structure
additional information dehydratase and isomerase activities of the bifunctional Ldi are only detectable in the presence of a reductant (dithiothreitol) and in the absence of O2 Castellaniella defragrans

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
 Castellaniella defragrans
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(3S)-linalool Castellaniella defragrans
-
 beta-myrcene + H2O
-
 r
(3S)-linalool Castellaniella defragrans 65Phen
-
 beta-myrcene + H2O
-
 r

Organism

Organism UniProt Comment Textmining
Castellaniella defragrans E1XUJ2
-
-
Castellaniella defragrans 65Phen E1XUJ2
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by hydrophobic interaction and anion exchange chromatography, and gel filtration Castellaniella defragrans

Reaction

Reaction Comment Organism Reaction ID
(3S)-linalool = myrcene + H2O the substrates are embedded inside a hydrophobic channel between two monomers of the (alpha,alpha)6 barrel fold class and flanked by three clusters of polar residues involved in acid-base catalysis. Catalytic mechanism, structure-function analysis, overview Castellaniella defragrans
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(3S)-linalool
-
 Castellaniella defragrans beta-myrcene + H2O
-
 r
(3S)-linalool
-
 Castellaniella defragrans 65Phen beta-myrcene + H2O
-
 r
additional information the bifunctional linalool dehydratase isomerase (LinD) catalyzes the isomerization of geraniol to linalool, EC 5.4.4.4, and likewise the dehydration of linalool to myrcene, EC 4.2.1.127. Substrate binding structure, overview Castellaniella defragrans ?
-
 ?
additional information the bifunctional linalool dehydratase isomerase (LinD) catalyzes the isomerization of geraniol to linalool, EC 5.4.4.4, and likewise the dehydration of linalool to myrcene, EC 4.2.1.127. Substrate binding structure, overview Castellaniella defragrans 65Phen ?
-
 ?

Subunits

Subunits Comment Organism
homopentamer gel filtration and crystal structure analysis, SDS-PAGE Castellaniella defragrans
More the crystal structure of Ldi reveals a cyclic homopentameric protein complex. Each monomer consists of a classical (alpha,alpha)6 barrel fold composed of six inner helices (63-80, 124-139, 179-193, 238-251, 294-306, and 341-351) flanked by six lateral helices (25-35, 85-100, 146-163, 198-212, 255-266 and 309-322) oriented in an antiparallel fashion Castellaniella defragrans

Synonyms

Synonyms Comment Organism
LDI
-
 Castellaniella defragrans
linalool dehydratase/isomerase
-
 Castellaniella defragrans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Castellaniella defragrans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Castellaniella defragrans

Cofactor

Cofactor Comment Organism Structure
additional information no enzyme-bound cofactors Castellaniella defragrans

General Information

General Information Comment Organism
additional information the substrates are embedded inside a hydrophobic channel between two monomers of the (alpha,alpha)6 barrel fold class and flanked by three clusters of polar residues involved in acid-base catalysis, modelling of the cytosolic enzyme domain. The substrate binding site in (alpha,alpha)6 barrel enzymes is embedded inside a cavity at the barrel entrance whereas the substrate cavity in Ldi is partly capped by the irregular segment 36'-52' of the neighbor monomer of the homopentamer Castellaniella defragrans
physiological function linalool dehydratase/isomerase (Ldi), an enzyme of terpene degradation in Castellaniella defragrans, isomerizes the primary monoterpene alcohol geraniol into the tertiary alcohol (3S)-linalool and dehydrates (3S)-linalool to the alkene beta-myrcene Castellaniella defragrans