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Literature summary extracted from

  • Demming, R.M.; Fischer, M.P.; Schmid, J.; Hauer, B.
    (De)hydratases-recent developments and future perspectives (2018), Curr. Opin. Chem. Biol., 43, 43-50 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.2.1.127 DMSO 10% v/v Castellaniella defragrans

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.127 gene ldi, DNA and amino acid sequence determination and analysis Castellaniella defragrans

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.127 additional information no inhibition by EDTA Castellaniella defragrans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.2.1.127 periplasm the enzyme sequence includes an N-terminal signal peptide of 27 amino acids suggesting that LinD is naturally transported into the periplasm Castellaniella defragrans
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.127 additional information the enzyme does not require metal atoms 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 LinD enantioselectively transforms beta-myrcene to (S)-(+)-linalool (coriandrol) with an enantiomeric excess of at least 95.4% beta-myrcene + H2O
-
r
4.2.1.127 (3S)-linalool Castellaniella defragrans 65Phen LinD enantioselectively transforms beta-myrcene to (S)-(+)-linalool (coriandrol) with an enantiomeric excess of at least 95.4% beta-myrcene + H2O
-
r
4.2.1.127 additional information Castellaniella defragrans 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 ?
-
?
4.2.1.127 additional information Castellaniella defragrans 65Phen 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 ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.127 Castellaniella defragrans E1XUJ2
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-
4.2.1.127 Castellaniella defragrans 65Phen E1XUJ2
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-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.127 native enzyme LinD out of crude extracts of strain 65Phen with a yield of 0.02% of the total soluble extract Castellaniella defragrans

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.127 (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 Castellaniella defragrans

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.127 0.00087
-
partially purified native enzyme, pH 8.0, 35°C, dehydratase activity 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 LinD enantioselectively transforms beta-myrcene to (S)-(+)-linalool (coriandrol) with an enantiomeric excess of at least 95.4% Castellaniella defragrans beta-myrcene + H2O
-
r
4.2.1.127 (3S)-linalool
-
Castellaniella defragrans 65Phen beta-myrcene + H2O
-
r
4.2.1.127 (3S)-linalool LinD enantioselectively transforms beta-myrcene to (S)-(+)-linalool (coriandrol) with an enantiomeric excess of at least 95.4% 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. 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 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. 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 Castellaniella defragrans 65Phen ?
-
?

Subunits

EC Number Subunits Comment Organism
4.2.1.127 homotetramer 4 * 40000, SDS-PAGE Castellaniella defragrans

Synonyms

EC Number Synonyms Comment Organism
4.2.1.127 LDI
-
Castellaniella defragrans
4.2.1.127 linalool dehydratase isomerase
-
Castellaniella defragrans
4.2.1.127 LinD
-
Castellaniella defragrans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.127 35
-
-
Castellaniella defragrans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.127 8
-
-
Castellaniella defragrans

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.2.1.127 additional information
-
pH optimum at low alkaline pH, showing a massive drop at pH beyond pH 9.0 Castellaniella defragrans

General Information

EC Number General Information Comment Organism
4.2.1.127 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 Castellaniella defragrans
4.2.1.127 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 Castellaniella defragrans