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(3S)-linalool = myrcene + H2O
(3S)-linalool = myrcene + H2O
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(3S)-linalool = myrcene + H2O
reaction mechanism, overview
(3S)-linalool = myrcene + H2O
catalytic mechanism of enzyme LinD by a combined quantum mechanics and molecular mechanics (QM/MM), computational modeling
(3S)-linalool = myrcene + H2O
reaction mechanism via one acid-base mechanism via a carbocation intermediate. Residues C171, Y45 and D39 act as general acid and base for the protonation of the hydroxyl leaving group of the substrate (S)-linalool and the dehydration at the chiral carbon atom. Water is activated by H129 or C180 and added to the covalent or carbocation intermediate
(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
(3S)-linalool = myrcene + H2O
reaction mechanism via one acid-base mechanism via a carbocation intermediate. Residues C171, Y45 and D39 act as general acid and base for the protonation of the hydroxyl leaving group of the substrate (S)-linalool and the dehydration at the chiral carbon atom. Water is activated by H129 or C180 and added to the covalent or carbocation intermediate
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(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
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(3S)-linalool
beta-myrcene + H2O
(6E)-3,7,11-trimethyldodeca-1,6,10-trien-3-ol
(6E)-7,11-dimethyl-3-methylidenedodeca-1,6,10-triene + H2O
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r
(E)-3-methylocta-1,4-dien-3-ol
(4E)-3-methylideneocta-1,4-diene + H2O
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r
(E/Z)-4,8-dimethylnona-2,7-dien-4-ol
(7E)-2-methyl-6-methylidenenona-2,7-diene + H2O
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r
(R,S)-linalool
beta-myrcene + H2O
2-methylbut-3-en-2-ol
2-methylbuta-1,3-diene + H2O
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r
3-ethyloct-1-en-3-ol
(3E)-3-ethylidene-7-methylocta-1,6-diene + H2O
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r
3-methoxy-3,7-dimethylocta-1,6-diene
beta-myrcene
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r
3-methyl-5-phenylpent-1-en-3-ol
(3-methylidenepent-4-en-1-yl)benzene + H2O
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r
3-methylhept-1-en-3-ol
3-methylidenehept-1-ene + H2O
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r
3-methylhex-1-en-3-ol
3-methylidenehex-1-ene + H2O
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r
beta-myrcene + H2O
(3S)-linalool
additional information
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(3S)-linalool
beta-myrcene + H2O
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r
(3S)-linalool
beta-myrcene + H2O
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r
(3S)-linalool
beta-myrcene + H2O
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r
(3S)-linalool
beta-myrcene + H2O
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(3S)-linalool
beta-myrcene + H2O
LinD enantioselectively transforms beta-myrcene to (S)-(+)-linalool (coriandrol) with an enantiomeric excess of at least 95.4%
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(3S)-linalool
beta-myrcene + H2O
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r
(3S)-linalool
beta-myrcene + H2O
LinD enantioselectively transforms beta-myrcene to (S)-(+)-linalool (coriandrol) with an enantiomeric excess of at least 95.4%
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(3S)-linalool
beta-myrcene + H2O
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(R,S)-linalool
beta-myrcene + H2O
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(R,S)-linalool
beta-myrcene + H2O
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the enzyme is not stereospecific
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r
(R,S)-linalool
beta-myrcene + H2O
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r
(R,S)-linalool
beta-myrcene + H2O
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the enzyme is not stereospecific
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r
beta-myrcene + H2O
(3S)-linalool
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beta-myrcene + H2O
(3S)-linalool
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beta-myrcene + H2O
(3S)-linalool
stereospecific reaction, introduction of the hydroxy group on the si-face of beta-myrcene
(3S)-linalool is formed with an enantiomeric excess of at least 95.4%, (3R)-inalool is not detected
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beta-myrcene + H2O
(3S)-linalool
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beta-myrcene + H2O
(3S)-linalool
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beta-myrcene + H2O
(3S)-linalool
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beta-myrcene + H2O
(3S)-linalool
stereospecific reaction, introduction of the hydroxy group on the si-face of beta-myrcene
(3S)-linalool is formed with an enantiomeric excess of at least 95.4%, (3R)-inalool is not detected
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linalool
myrcene + H2O
dehydration of linalool to myrcene in the absence of molecular oxygen. The aerobically purified enzyme is anaerobically activated in the presence of 2 mM dithiothreitol. The enzyme catalyzes in vitro the reaction in both directions depending on the thermodynamic driving forces
myrcene is the only product detected
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r
linalool
myrcene + H2O
dehydration of linalool to myrcene in the absence of molecular oxygen. The aerobically purified enzyme is anaerobically activated in the presence of 2 mM dithiothreitol. The enzyme catalyzes in vitro the reaction in both directions depending on the thermodynamic driving forces
myrcene is the only product detected
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r
myrcene + H2O
linalool
degradation of myrcene
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r
myrcene + H2O
linalool
degradation of myrcene
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r
additional information
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neither the monoterpenes alpha- and beta-ocimene nor the monoterpenoids citronellol and nerol are transformed
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additional information
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the thermodynamically favoured direction is the isomerization of geraniol to linalool and the dehydration reaction to beta-myrcene
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additional information
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the thermodynamically favoured direction is the isomerization of geraniol to linalool and the dehydration reaction to beta-myrcene
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additional information
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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
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additional information
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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
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additional information
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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. No activity with alpha-ocimene and beta-ocimene as well as citronellol and nerol. LinD accepts a broad variety of elongated and truncated aliphatic and even aromatic tertiary alcohols (C5-C15) providing chiral dehydration products with selectivity factors of up to 200. Substrates lacking the signature motif are not accepted by LinD
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additional information
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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 beta-myrcene, EC 4.2.1.127
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additional information
?
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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 beta-myrcene, EC 4.2.1.127
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additional information
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enzyme LinD shows a broad substrate specificity, truncated and elongated aromatic and aliphatic tertiary alcohols (C5-C15) that contain a specific signature motif can be substrates, structural requirements for substrates, overview. GC/MS analysis of linalool methyl ether conversion with LinD. No dehydratase activity with 2,6-dimethylhept-5-en-2-ol, 3,7-dimethyloct-6-en-3-ol, (E)-3-methyloct-4-en-3-ol, (E)-3,7-dimethyl-1,4,6-trien-3-ol, (E)-3,7-dimethylocta-4,6-dien-3-ol, 7-methylocta-1,6-dien-3-ol, 3,7-dimethylocta-1,6-dien-3-amine (i.e. linalyl amine), and 3,7-dimethyloct-6-en-1-yn-3-ol. Compounds 3-methylbut-2-en-1-ol, (2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ol, and geraniol are substrates for the isomerization activity of the enzyme
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additional information
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enzyme LinD shows a broad substrate specificity, truncated and elongated aromatic and aliphatic tertiary alcohols (C5-C15) that contain a specific signature motif can be substrates, structural requirements for substrates, overview. GC/MS analysis of linalool methyl ether conversion with LinD. No dehydratase activity with 2,6-dimethylhept-5-en-2-ol, 3,7-dimethyloct-6-en-3-ol, (E)-3-methyloct-4-en-3-ol, (E)-3,7-dimethyl-1,4,6-trien-3-ol, (E)-3,7-dimethylocta-4,6-dien-3-ol, 7-methylocta-1,6-dien-3-ol, 3,7-dimethylocta-1,6-dien-3-amine (i.e. linalyl amine), and 3,7-dimethyloct-6-en-1-yn-3-ol. Compounds 3-methylbut-2-en-1-ol, (2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ol, and geraniol are substrates for the isomerization activity of the enzyme
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additional information
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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
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?
additional information
?
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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
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?
additional information
?
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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. No activity with alpha-ocimene and beta-ocimene as well as citronellol and nerol. LinD accepts a broad variety of elongated and truncated aliphatic and even aromatic tertiary alcohols (C5-C15) providing chiral dehydration products with selectivity factors of up to 200. Substrates lacking the signature motif are not accepted by LinD
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additional information
?
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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
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additional information
?
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neither the monoterpenes alpha- and beta-ocimene nor the monoterpenoids citronellol and nerol are transformed
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?
additional information
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the thermodynamically favoured direction is the isomerization of geraniol to linalool and the dehydration reaction to beta-myrcene
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?
additional information
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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
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?
additional information
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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
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(3S)-linalool
beta-myrcene + H2O
(R,S)-linalool
beta-myrcene + H2O
beta-myrcene + H2O
(3S)-linalool
additional information
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(3S)-linalool
beta-myrcene + H2O
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r
(3S)-linalool
beta-myrcene + H2O
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r
(3S)-linalool
beta-myrcene + H2O
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r
(3S)-linalool
beta-myrcene + H2O
LinD enantioselectively transforms beta-myrcene to (S)-(+)-linalool (coriandrol) with an enantiomeric excess of at least 95.4%
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r
(3S)-linalool
beta-myrcene + H2O
LinD enantioselectively transforms beta-myrcene to (S)-(+)-linalool (coriandrol) with an enantiomeric excess of at least 95.4%
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r
(3S)-linalool
beta-myrcene + H2O
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(R,S)-linalool
beta-myrcene + H2O
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(R,S)-linalool
beta-myrcene + H2O
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r
beta-myrcene + H2O
(3S)-linalool
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beta-myrcene + H2O
(3S)-linalool
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beta-myrcene + H2O
(3S)-linalool
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beta-myrcene + H2O
(3S)-linalool
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beta-myrcene + H2O
(3S)-linalool
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myrcene + H2O
linalool
degradation of myrcene
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r
myrcene + H2O
linalool
degradation of myrcene
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r
additional information
?
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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
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?
additional information
?
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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
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?
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. No activity with alpha-ocimene and beta-ocimene as well as citronellol and nerol. LinD accepts a broad variety of elongated and truncated aliphatic and even aromatic tertiary alcohols (C5-C15) providing chiral dehydration products with selectivity factors of up to 200. Substrates lacking the signature motif are not accepted by LinD
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?
additional information
?
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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 beta-myrcene, EC 4.2.1.127
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?
additional information
?
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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 beta-myrcene, EC 4.2.1.127
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-
?
additional information
?
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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. No activity with alpha-ocimene and beta-ocimene as well as citronellol and nerol. LinD accepts a broad variety of elongated and truncated aliphatic and even aromatic tertiary alcohols (C5-C15) providing chiral dehydration products with selectivity factors of up to 200. Substrates lacking the signature motif are not accepted by LinD
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?
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malfunction
an in-frame deletion mutant with an inactivated ldi gene shows no growth with the acyclic beta-myrcene, but grows like the wild type on limonene or alpha-phellandrene
malfunction
deletion of gene ldi affects growth on acyclic monoterpenes, e.g. beta-myrcene, phenotype, overview
malfunction
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deletion of gene ldi affects growth on acyclic monoterpenes, e.g. beta-myrcene, phenotype, overview
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malfunction
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an in-frame deletion mutant with an inactivated ldi gene shows no growth with the acyclic beta-myrcene, but grows like the wild type on limonene or alpha-phellandrene
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metabolism
beta-myrcene is enantiospecifically hydrated to (S)-(+)-linalool and further isomerized to geraniol by the linalool dehydrataseisomerase
metabolism
the bifunctional linalool dehydratase-isomerase ldi/LDI is the initial enzyme in the anaerobic beta-myrcene degradation pathway and catalyzes the hydration of beta-myrcene to (S)-(+)-linalool and its isomerization to geraniol. A high-affinity geraniol dehydrogenase geoA/GeDH and a geranial dehydrogenase geoB/GaDH contribute to the formation of geranic acid
metabolism
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the bifunctional linalool dehydratase-isomerase ldi/LDI is the initial enzyme in the anaerobic beta-myrcene degradation pathway and catalyzes the hydration of beta-myrcene to (S)-(+)-linalool and its isomerization to geraniol. A high-affinity geraniol dehydrogenase geoA/GeDH and a geranial dehydrogenase geoB/GaDH contribute to the formation of geranic acid
metabolism
the enzyme is responsible for the first two steps in myrcene degradation in Castellaniella defragrans as geraniol is further oxidized shifting the reaction equilibrium
metabolism
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the enzyme is responsible for the first two steps in myrcene degradation in Castellaniella defragrans as geraniol is further oxidized shifting the reaction equilibrium
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metabolism
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the bifunctional linalool dehydratase-isomerase ldi/LDI is the initial enzyme in the anaerobic beta-myrcene degradation pathway and catalyzes the hydration of beta-myrcene to (S)-(+)-linalool and its isomerization to geraniol. A high-affinity geraniol dehydrogenase geoA/GeDH and a geranial dehydrogenase geoB/GaDH contribute to the formation of geranic acid
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metabolism
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beta-myrcene is enantiospecifically hydrated to (S)-(+)-linalool and further isomerized to geraniol by the linalool dehydrataseisomerase
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physiological function
essential requirement of the linalool dehydratase-isomerase for growth on acyclic monoterpenes, e.g. beta-myrcene, but not on cyclic monoterpenes, e.g. cyclic alpha-phellandrene or limonene
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
physiological function
the bifunctional linalool dehydratase isomerase (LinD) from the bacterium Castellaniella defragrans catalyzes in nature the hydration of beta-myrcene to (3S)-linalool and the subsequent isomerization to geraniol
physiological function
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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 (3S)-linalool and dehydrates (3S)-linalool to the alkene beta-myrcene
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physiological function
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essential requirement of the linalool dehydratase-isomerase for growth on acyclic monoterpenes, e.g. beta-myrcene, but not on cyclic monoterpenes, e.g. cyclic alpha-phellandrene or limonene
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additional information
growth on cyclic monoterpenes independent of the initial enzyme linalool dehydratase suggests the presence of a second enzyme system activating unsaturated hydrocarbons
additional information
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growth on cyclic monoterpenes independent of the initial enzyme linalool dehydratase suggests the presence of a second enzyme system activating unsaturated hydrocarbons
additional information
catalytic mechanism of enzyme LinD by a combined quantum mechanics and molecular mechanics (QM/MM), computational modeling resulting in two models. Model I (LinD-linalool) is derived from the crystal structure of the selenomethionine derivative of LinD (SeMet-LinD) in complex with the natural substrate geraniol, whereas model II (LinD-beta-myrcene) is constructed from the crystal structure of LinD in complex with beta-myrcene. Model II as the active one, which implies that hydration and dehydration are sensitive to the protonation state and fine structure of the active site: Firstly, beta-myrcene is hydrated by a crystal water (W14) and is converted into the stable intermediate (3S)-linalool, then linalool is isomerized to geraniol with an overall energy barrier of 24.6 kcal/mol. Besides, linalool can also reversibly convert into the reactant with an energy barrier of 24.1 kcal/mol. The intermediate IM1 can directly transform to geraniol without first converting to (3S)-linalool. His128 and Tyr65 form hydrogen bonds to stabilize the structure of the active site, but they do not act as general acid/base catalysts during the catalytic reactions
additional information
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catalytic mechanism of enzyme LinD by a combined quantum mechanics and molecular mechanics (QM/MM), computational modeling resulting in two models. Model I (LinD-linalool) is derived from the crystal structure of the selenomethionine derivative of LinD (SeMet-LinD) in complex with the natural substrate geraniol, whereas model II (LinD-beta-myrcene) is constructed from the crystal structure of LinD in complex with beta-myrcene. Model II as the active one, which implies that hydration and dehydration are sensitive to the protonation state and fine structure of the active site: Firstly, beta-myrcene is hydrated by a crystal water (W14) and is converted into the stable intermediate (3S)-linalool, then linalool is isomerized to geraniol with an overall energy barrier of 24.6 kcal/mol. Besides, linalool can also reversibly convert into the reactant with an energy barrier of 24.1 kcal/mol. The intermediate IM1 can directly transform to geraniol without first converting to (3S)-linalool. His128 and Tyr65 form hydrogen bonds to stabilize the structure of the active site, but they do not act as general acid/base catalysts during the catalytic reactions
additional information
structure of LinD in complex with the prodxaduct geraniol, structure-function relationship, overview. Cys171 is well positioned to protonate the linalool hydroxyl of the (S)-configuration, and a covalent LinD-terpene complex is formed as the hydroxyl is eliminated as water. The covalent intermediate underxadgoes either hydrolysis, by a water molecule activated by His129, to give geraniol in an isomerization reaction, or base-catalyzed elimixadnation, most likely by Asp39 or Tyr45 at the methyl group, to give myrcene in a dehydration process. In the second proposal, involvxading a carbocation intermediate, Cys180 does not interact directly with the substrate terminal C=C double bond. Dehydration of (3S)-linalool, catalyzed by Cys171, results in a carbocation intermediate that undergoes either rehydration, catalyzed by His129 or Cys180 to form geraniol, or base-catalyzed deprotonation to form myrcene by Tyr45 and Asp39
additional information
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structure of LinD in complex with the prodxaduct geraniol, structure-function relationship, overview. Cys171 is well positioned to protonate the linalool hydroxyl of the (S)-configuration, and a covalent LinD-terpene complex is formed as the hydroxyl is eliminated as water. The covalent intermediate underxadgoes either hydrolysis, by a water molecule activated by His129, to give geraniol in an isomerization reaction, or base-catalyzed elimixadnation, most likely by Asp39 or Tyr45 at the methyl group, to give myrcene in a dehydration process. In the second proposal, involvxading a carbocation intermediate, Cys180 does not interact directly with the substrate terminal C=C double bond. Dehydration of (3S)-linalool, catalyzed by Cys171, results in a carbocation intermediate that undergoes either rehydration, catalyzed by His129 or Cys180 to form geraniol, or base-catalyzed deprotonation to form myrcene by Tyr45 and Asp39
additional information
the active site of the enzyme is proposed to be located at the interface of two neighboring monomers and, therefore, to be made up of amino acid residues M125, C171, C180, H129, Q179 and Y420 from chain A and D39 and Y45 from chain B. Residues Y45, M125, H129, C171 and C180 are involved in the mechanism of the isomerization of geraniol as well as the dehydration of linalool. Reaction mechanisms, one via a covalent intermediate, and one acid-base mechanism via a carbocation intermediate. In both cases, C171, Y45 and D39 act as general acid and base for the protonation of the hydroxyl leaving group of the substrate (S)-linalool and the dehydration at the chiral carbon atom. Water is activated by H129 or C180 and added to the covalent or carbocation intermediate
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
additional information
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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
additional information
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the active site of the enzyme is proposed to be located at the interface of two neighboring monomers and, therefore, to be made up of amino acid residues M125, C171, C180, H129, Q179 and Y420 from chain A and D39 and Y45 from chain B. Residues Y45, M125, H129, C171 and C180 are involved in the mechanism of the isomerization of geraniol as well as the dehydration of linalool. Reaction mechanisms, one via a covalent intermediate, and one acid-base mechanism via a carbocation intermediate. In both cases, C171, Y45 and D39 act as general acid and base for the protonation of the hydroxyl leaving group of the substrate (S)-linalool and the dehydration at the chiral carbon atom. Water is activated by H129 or C180 and added to the covalent or carbocation intermediate
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additional information
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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
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additional information
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growth on cyclic monoterpenes independent of the initial enzyme linalool dehydratase suggests the presence of a second enzyme system activating unsaturated hydrocarbons
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?
x * 43000, recombinant wild-type enzyme, SDS-PAGE
decamer
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10 x 60000, recombinant enzyme, SDS-PAGE, 10 x 71800, about, sequence calculation
decamer
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10 x 60000, recombinant enzyme, SDS-PAGE, 10 x 71800, about, sequence calculation
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homopentamer
gel filtration and crystal structure analysis, SDS-PAGE
homopentamer
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gel filtration and crystal structure analysis, SDS-PAGE
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homotetramer
4 * 40000, SDS-PAGE
homotetramer
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4 * 40000, SDS-PAGE
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tetramer
4 * 40000, SDS-PAGE
tetramer
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4 * 40000, SDS-PAGE
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additional information
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
additional information
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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
additional information
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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
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C171A
site-directed mutagenesis, inactive mutant
C180A
site-directed mutagenesis, inactive mutant
H129A
site-directed mutagenesis, the mutant shows 23% epimerase and 6% dehydratase, respectively, compared to the wild-type
M125A
site-directed mutagenesis, the mutant shows 2% epimerase and no dehydratase, respectively, compared to the wild-type
Y45F
site-directed mutagenesis, the mutant shows 22% epimerase and no dehydratase, respectively, compared to the wild-type
additional information
generation of an in-frame deletion mutants Castellaniella defragrans DELTAldi
additional information
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generation of an in-frame deletion mutants Castellaniella defragrans DELTAldi
additional information
generation of an in-frame deletion mutants Castellaniella defragrans DELTAldi
additional information
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generation of an in-frame deletion mutants Castellaniella defragrans DELTAldi
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additional information
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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
additional information
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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
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Brodkorb, D.; Gottschall, M.; Marmulla, R.; Lddeke, F.; Harder, J.
Linalool dehydratase-isomerase, a bifunctional enzyme in the anaerobic degradation of monoterpenes
J. Biol. Chem.
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30436-30442
2010
Castellaniella defragrans (E1XUJ2), Castellaniella defragrans 65Phen (E1XUJ2)
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Physiology of deletion mutants in the anaerobic beta-myrcene degradation pathway in Castellaniella defragrans
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Enantiospecific (S)-(+)-linalool formation from beta-myrcene by linalool dehydratase-isomerase
Z. Naturforsch. C
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2011
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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
BMC Biochem.
17
6
2016
Thauera linaloolentis, Thauera linaloolentis 47Lol
brenda
Demming, R.M.; Fischer, M.P.; Schmid, J.; Hauer, B.
(De)hydratases-recent developments and future perspectives
Curr. Opin. Chem. Biol.
43
43-50
2018
Castellaniella defragrans (E1XUJ2), Castellaniella defragrans 65Phen (E1XUJ2)
brenda
Weidenweber, S.; Marmulla, R.; Ermler, U.; Harder, J.
X-ray structure of linalool dehydratase/isomerase from Castellaniella defragrans reveals enzymatic alkene synthesis
FEBS Lett.
590
1375-1383
2016
Castellaniella defragrans (E1XUJ2), Castellaniella defragrans, Castellaniella defragrans 65Phen (E1XUJ2)
brenda
Nestl, B.M.; Geinitz, C.; Popa, S.; Rizek, S.; Haselbeck, R.J.; Stephen, R.; Noble, M.A.; Fischer, M.P.; Ralph, E.C.; Hau, H.T.; Man, H.; Omar, M.; Turkenburg, J.P.; van Dien, S.; Culler, S.J.; Grogan, G.; Hauer, B.
Structural and functional insights into asymmetric enzymatic dehydration of alkenols
Nat. Chem. Biol.
13
275-281
2017
Castellaniella defragrans (E1XUJ2), Castellaniella defragrans
brenda
Ling, B.; Wang, X.; Su, H.; Liu, R.; Liu, Y.
Protonation state and fine structure of the active site determine the reactivity of dehydratase hydration and isomerization of beta-myrcene catalyzed by linalool dehydratase/isomerase from Castellaniella defragrans
Phys. Chem. Chem. Phys.
20
17342-17352
2018
Castellaniella defragrans (E1XUJ2), Castellaniella defragrans
brenda