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Literature summary extracted from

  • Marmulla, R.; Safaric, B.; Markert, S.; Schweder, T.; Harder, J.
    Linalool isomerase, a membrane-anchored enzyme in the anaerobic monoterpene degradation in Thauera linaloolentis 47Lol (2016), BMC Biochem., 17, 6 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.2.1.127 additional information enzyme activity requires a reductant for activation, influence of different reducing agents on Lis activity, overview Thauera linaloolentis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.127 gene lis, recombinant expression in Escherichia coli strain BL21(DE3) in membranes Thauera linaloolentis

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.127 additional information expression of a N-terminally truncated version of the linalool isomerase, representing the cytosolic part of the enzyme only, yields a soluble protein that does not show activity Thauera linaloolentis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.127 additional information detergent-mediated release of the protein from the membrane causes irreversible inhibitory effects on the enzyme activity Thauera linaloolentis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.127 additional information
-
 additional information Michaelis-Menten-kinetics Thauera linaloolentis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.2.1.127 inner membrane membrane-anchored enzyme Thauera linaloolentis
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.127 600000
-
 gel filtration Thauera linaloolentis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.127 (R,S)-linalool Thauera linaloolentis
-
 beta-myrcene + H2O
-
 r
4.2.1.127 (R,S)-linalool Thauera linaloolentis 47Lol
-
 beta-myrcene + H2O
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.127 Thauera linaloolentis
-
-
-
4.2.1.127 Thauera linaloolentis 47Lol
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.127 native enzyme from the inner membrane using subcellular fractionation including a sucrose-gradient centrifugation and ultracentrifugation at 150000 x g, anion exchange and hydrophobic interaction chromatography, and gel filtration, the detergent-mediated release of the protein from the membrane has irreversible inhibitory effects on the enzyme activity, spheroplast preparation Thauera linaloolentis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.127 (R,S)-linalool
-
 Thauera linaloolentis beta-myrcene + H2O
-
 r
4.2.1.127 (R,S)-linalool the enzyme is not stereospecific Thauera linaloolentis beta-myrcene + H2O
-
 r
4.2.1.127 (R,S)-linalool
-
 Thauera linaloolentis 47Lol beta-myrcene + H2O
-
 r
4.2.1.127 (R,S)-linalool the enzyme is not stereospecific Thauera linaloolentis 47Lol beta-myrcene + H2O
-
 r
4.2.1.127 additional information a bifunctional linalool dehydratase/isomerase that exhibits dehydratase activity, Ec 4.2.1.127, and isomerase activity, EC 5.4.4.4. The enzyme catalyzes the reversible hydration of beta-myrcene to linalool and its isomerization to geraniol. No activity is measured with nerol or citronellol alone. Linalool isomerase activity drops to approx. 50% in the presence of nerol. Activity in the presence of citronellol and geraniol is barely detectable. The enzyme is regioselective and seems to bind nerol with a similar affinity as geraniol, whereas citronellol which lacks the C2-C3 double bond is stronger bound than geraniol. Stereoselectivity analysis Thauera linaloolentis ?
-
 ?
4.2.1.127 additional information a bifunctional linalool dehydratase/isomerase that exhibits dehydratase activity, Ec 4.2.1.127, and isomerase activity, EC 5.4.4.4. The enzyme catalyzes the reversible hydration of beta-myrcene to linalool and its isomerization to geraniol. No activity is measured with nerol or citronellol alone. Linalool isomerase activity drops to approx. 50% in the presence of nerol. Activity in the presence of citronellol and geraniol is barely detectable. The enzyme is regioselective and seems to bind nerol with a similar affinity as geraniol, whereas citronellol which lacks the C2-C3 double bond is stronger bound than geraniol. Stereoselectivity analysis Thauera linaloolentis 47Lol ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.127 decamer 10 x 60000, recombinant enzyme, SDS-PAGE, 10 x 71800, about, sequence calculation Thauera linaloolentis

Synonyms

EC Number Synonyms Comment Organism
4.2.1.127 linalool dehydratase/isomerase
-
 Thauera linaloolentis
4.2.1.127 LIS
-
 Thauera linaloolentis
4.2.1.127 More cf. EC 5.4.4.4 Thauera linaloolentis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.127 28
-
 assay at Thauera linaloolentis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.127 8
-
 assay at Thauera linaloolentis