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Literature summary for 4.2.1.127 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
Search for more literature for 4.2.1.127

Activating Compound

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

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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

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

KM Value [mM]

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

Localization

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Thauera linaloolentis
-
-
-
Thauera linaloolentis 47Lol
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R,S)-linalool
-
 Thauera linaloolentis beta-myrcene + H2O
-
 r
(R,S)-linalool the enzyme is not stereospecific Thauera linaloolentis beta-myrcene + H2O
-
 r
(R,S)-linalool
-
 Thauera linaloolentis 47Lol beta-myrcene + H2O
-
 r
(R,S)-linalool the enzyme is not stereospecific Thauera linaloolentis 47Lol beta-myrcene + H2O
-
 r
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 ?
-
 ?
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

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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