Any feedback?
Information on EC 4.2.1.127 - linalool dehydratase and Organism(s) Castellaniella defragrans and UniProt Accession E1XUJ2
for references in articles please use BRENDA:EC4.2.1.127Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.2.1.127 linalool dehydrataseIUBMB Comments
In absence of oxygen the bifunctional linalool dehydratase-isomerase can catalyse in vitro two reactions, the hydration of myrcene to (3S)-linalool and the isomerization of (3S)-linalool to geraniol, the latter activity being classified as EC 5.4.4.4, geraniol isomerase.
Specify your search results
Word Map
- 4.2.1.127
- castellaniella
- defragrans
-
isomerization
-
monoterpene
-
acyclic
-
s-+-linalool
- alkene
-
in-frame
-
terpene
-
betaproteobacterium
- beta-myrcene
- biotechnology
- synthesis
The taxonomic range for the selected organisms is: Castellaniella defragrans
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
linalool dehydratase-isomerase, linalool dehydratase/isomerase, linalool dehydratase, ldi/ldi, linalool dehydratase isomerase, bifunctional linalool dehydratase isomerase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
linalool dehydratase-isomerase
additional information
linalool dehydratase-isomerase
bifunctional enzyme that catalyzes the reversible dehydration and isomerization of linalool (3,7-dimethyl-1,6-octadien-3-ol)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(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
SYSTEMATIC NAME
IUBMB Comments
linalool hydro-lyase (myrcene-forming)
In absence of oxygen the bifunctional linalool dehydratase-isomerase can catalyse in vitro two reactions, the hydration of myrcene to (3S)-linalool and the isomerization of (3S)-linalool to geraniol, the latter activity being classified as EC 5.4.4.4, geraniol isomerase.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(6E)-3,7,11-trimethyldodeca-1,6,10-trien-3-ol
(6E)-7,11-dimethyl-3-methylidenedodeca-1,6,10-triene + H2O
-
-
-
r
(E)-3-methylocta-1,4-dien-3-ol
(4E)-3-methylideneocta-1,4-diene + H2O
-
-
-
r
(E/Z)-4,8-dimethylnona-2,7-dien-4-ol
(7E)-2-methyl-6-methylidenenona-2,7-diene + H2O
-
-
-
r
3-ethyloct-1-en-3-ol
(3E)-3-ethylidene-7-methylocta-1,6-diene + H2O
-
-
-
r
3-methyl-5-phenylpent-1-en-3-ol
(3-methylidenepent-4-en-1-yl)benzene + H2O
-
-
-
r
3-methylhept-1-en-3-ol
3-methylidenehept-1-ene + H2O
-
-
-
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
-
r
(3S)-linalool
beta-myrcene + H2O
LinD enantioselectively transforms beta-myrcene to (S)-(+)-linalool (coriandrol) with an enantiomeric excess of at least 95.4%
-
-
r
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
-
?
additional information
?
-
neither the monoterpenes alpha- and beta-ocimene nor the monoterpenoids citronellol and nerol are transformed
-
-
?
additional information
?
-
the thermodynamically favoured direction is the isomerization of geraniol to linalool and the dehydration reaction to beta-myrcene
-
-
?
additional information
?
-
-
the thermodynamically favoured direction is the isomerization of geraniol to linalool and the dehydration reaction to beta-myrcene
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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 beta-myrcene, EC 4.2.1.127
-
-
?
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 beta-myrcene, EC 4.2.1.127
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3S)-linalool
beta-myrcene + H2O
LinD enantioselectively transforms beta-myrcene to (S)-(+)-linalool (coriandrol) with an enantiomeric excess of at least 95.4%
-
-
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
-
-
?
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
-
-
?
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
-
-
?
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 beta-myrcene, EC 4.2.1.127
-
-
?
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 beta-myrcene, EC 4.2.1.127
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the enzyme does not require metal atoms
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KCl
high salt concentrations (NaCl, KCl, or MgCl2 at a concentration of 220 mM) inhibit the enzyme activity completely
linalyl amine
the simultaneous utilization of 10 mM (3S)-linalool and varying concentrations (0.01-10 mM) of linalyl amine in biotransformations results in almost complete inactixadvation (over 98%) of LinD even when the amine concentration is low
MgCl2
high salt concentrations (NaCl, KCl, or MgCl2 at a concentration of 220 mM) inhibit the enzyme activity completely
NaCl
high salt concentrations (NaCl, KCl, or MgCl2 at a concentration of 220 mM) inhibit the enzyme activity completely
O2
the enzyme requires dithiothreitol as a reducing agent and an oxygen free microenvironment (less than 1% (v/v)) for the dehydration of linalool
Urea
20% activity remains at 3 M urea, and no activity is detected in 6 M urea
additional information
not inhibited by 10% (v/v) DMSO. EDTA (5 mM) does not affect the enzyme activity
-
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
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
the aerobically purified enzyme is anaerobically activated in the presence of 2 mM dithiothreitol
additional information
the enzyme requires dithiothreitol as a reducing agent and an oxygen free microenvironment (less than 1% (v/v)) for the dehydration of linalool
-
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
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00087
partially purified native enzyme, pH 8.0, 35°C, dehydratase activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9
Tris-HCl buffer, sharp decrease in linalool dehydratase activity beyond pH 9.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH optimum at low alkaline pH, showing a massive drop at pH beyond pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28 - 40
28°C: about 60% of maximal activity, 40°C: about 80% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Alcaligenes defragrans, gene ldi
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
proteome analysis of cells grown on acetate and alpha-phellandrene by 2D-SDS-PAGE and LC-ESI-MS/MS of whole-cell homogenate and membrane protein-enriched fraction, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme sequence includes an N-terminal signal peptide of 27 amino acids suggesting that LinD is naturally transported into the periplasm
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
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
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
-
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
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
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
-
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
-
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
-
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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homopentamer
gel filtration and crystal structure analysis, SDS-PAGE
additional information
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
-
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
precursor protein with a signal peptide for a periplasmatic location
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of enzyme structure from crystal structure of the enzyme complexed with (S)-linalool, PDB ID 5G1U
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
purified wild-type enzyme LinD alone or in complex with geraniol, or as selenomethionine-labeled enzyme, X-ray diffraction structure determination and analysis at 1.76-2.68 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
generation of an in-frame deletion mutants Castellaniella defragrans DELTAldi
additional information
-
generation of an in-frame deletion mutants Castellaniella defragrans DELTAldi
additional information
generation of an in-frame deletion mutants Castellaniella defragrans DELTAldi
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme LinD out of crude extracts of strain 65Phen with a yield of 0.02% of the total soluble extract
recombinant enzyme from Escherichia coli strain BL21(DE3) by hydrophobic interaction and anion exchange chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ldi, DNA and amino acid sequence determination and analysis
gene ldi, recombinant expression in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
proteome analysis of cells grown on acetate and alpha-phellandrene by 2D-SDS-PAGE and LC-ESI-MS/MS of whole-cell homogenate and membrane protein-enriched fraction, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
possible biotechnological applications of Ldi, in particular, are industrial butadiene and isoprene production from renewable sources
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
285
30436-30442
2010
Castellaniella defragrans (E1XUJ2), Castellaniella defragrans 65Phen (E1XUJ2)
Lueddeke, F.; Dikfidan, A.; Harder, J.
Physiology of deletion mutants in the anaerobic beta-myrcene degradation pathway in Castellaniella defragrans
BMC Microbiol.
12
192
2012
Castellaniella defragrans (E1XUJ2), Castellaniella defragrans, Castellaniella defragrans 65Phen (E1XUJ2)
Petasch, J.; Disch, E.M.; Markert, S.; Becher, D.; Schweder, T.; Huettel, B.; Reinhardt, R.; Harder, J.
The oxygen-independent metabolism of cyclic monoterpenes in Castellaniella defragrans 65Phen
BMC Microbiol.
14
164
2014
Castellaniella defragrans (E1XUJ2), Castellaniella defragrans 65Phen (E1XUJ2), Castellaniella defragrans 65Phen
Lueddeke, F.; Harder, J.
Enantiospecific (S)-(+)-linalool formation from beta-myrcene by linalool dehydratase-isomerase
Z. Naturforsch. C
66
409-412
2011
Castellaniella defragrans (E1XUJ2), Castellaniella defragrans, Castellaniella defragrans 65Phen (E1XUJ2)
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)
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)
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
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
EXTERNAL LINKS (specific for EC-Number 4.2.1.127)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
