Any feedback?
Literature summary extracted from
- X-ray structure of linalool dehydratase/isomerase from Castellaniella defragrans reveals enzymatic alkene synthesis (2016), FEBS Lett., 590, 1375-1383 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.127 | DTT | a reductant is required for activity | Castellaniella defragrans |  |
| 4.2.1.127 | 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
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 4.2.1.127 | biotechnology | possible biotechnological applications of Ldi, in particular, are industrial butadiene and isoprene production from renewable sources | Castellaniella defragrans |
| 4.2.1.127 | 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)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.2.1.127 | gene ldi, recombinant expression in Escherichia coli strain BL21(DE3) | Castellaniella defragrans |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.2.1.127 | 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
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.127 | 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
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 4.2.1.127 | periplasm | - |
Castellaniella defragrans | - |
- |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.127 | (3S)-linalool | Castellaniella defragrans | - |
beta-myrcene + H2O | - |
r | |
| 4.2.1.127 | (3S)-linalool | Castellaniella defragrans 65Phen | - |
beta-myrcene + H2O | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.127 | Castellaniella defragrans | E1XUJ2 | - |
- |
| 4.2.1.127 | Castellaniella defragrans 65Phen | E1XUJ2 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.2.1.127 | recombinant enzyme from Escherichia coli strain BL21(DE3) by hydrophobic interaction and anion exchange chromatography, and gel filtration | Castellaniella defragrans |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 4.2.1.127 | (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 |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.127 | (3S)-linalool | - |
Castellaniella defragrans | beta-myrcene + H2O | - |
r | |
| 4.2.1.127 | (3S)-linalool | - |
Castellaniella defragrans 65Phen | beta-myrcene + H2O | - |
r | |
| 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. Substrate binding structure, overview | Castellaniella defragrans | ? | - |
? | |
| 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. Substrate binding structure, overview | Castellaniella defragrans 65Phen | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.2.1.127 | homopentamer | gel filtration and crystal structure analysis, SDS-PAGE | Castellaniella defragrans |
| 4.2.1.127 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.1.127 | LDI | - |
Castellaniella defragrans |
| 4.2.1.127 | linalool dehydratase/isomerase | - |
Castellaniella defragrans |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.127 | 22 | - |
assay at room temperature | Castellaniella defragrans |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.127 | 8 | - |
assay at | Castellaniella defragrans |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.127 | additional information | no enzyme-bound cofactors | Castellaniella defragrans |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.2.1.127 | 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 |
| 4.2.1.127 | 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 |
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
