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Literature summary for 4.2.1.127 extracted from

  • 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 (2018), Phys. Chem. Chem. Phys., 20, 17342-17352 .
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
analysis of enzyme structure from crystal structure of the enzyme complexed with (S)-linalool, PDB ID 5G1U Castellaniella defragrans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(3S)-linalool Castellaniella defragrans
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 beta-myrcene + H2O
-
 r
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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Castellaniella defragrans E1XUJ2
-
-

Reaction

Reaction Comment Organism Reaction ID
(3S)-linalool = myrcene + H2O catalytic mechanism of enzyme LinD by a combined quantum mechanics and molecular mechanics (QM/MM), computational modeling Castellaniella defragrans
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(3S)-linalool
-
 Castellaniella defragrans beta-myrcene + H2O
-
 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 Castellaniella defragrans ?
-
 ?

Synonyms

Synonyms Comment Organism
LDI
-
 Castellaniella defragrans
linalool dehydratase/isomerase
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 Castellaniella defragrans
LinD
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 Castellaniella defragrans
More cf. EC 5.4.4.4 Castellaniella defragrans

General Information

General Information Comment Organism
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 Castellaniella defragrans