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Information on EC 5.4.4.4 - geraniol isomerase for references in articles please use BRENDA:EC5.4.4.4
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EC Tree
IUBMB Comments In absence of oxygen the bifunctional linalool dehydratase-isomerase can catalyse in vitro two reactions, the isomerization of (3S)-linalool to geraniol and the hydration of myrcene to (3S)-linalool, the latter activity being classified as EC 4.2.1.127, linalool dehydratase.
The expected taxonomic range for this enzyme is: Castellaniella defragrans
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geraniol = (3S)-linalool
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geraniol hydroxymutase
In absence of oxygen the bifunctional linalool dehydratase-isomerase can catalyse in vitro two reactions, the isomerization of (3S)-linalool to geraniol and the hydration of myrcene to (3S)-linalool, the latter activity being classified as EC 4.2.1.127, linalool dehydratase.
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geraniol
linalool
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r
geraniol
linalool
the aerobically purified enzyme is anaerobically activated in the presence of 2 mM dithiothreitol. The enzyme catalyses in vitro the reaction in both directions depending on the thermodynamic driving forces
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r
geraniol
linalool
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r
geraniol
linalool
the aerobically purified enzyme is anaerobically activated in the presence of 2 mM dithiothreitol. The enzyme catalyses in vitro the reaction in both directions depending on the thermodynamic driving forces
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r
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geraniol
linalool
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r
geraniol
linalool
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r
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additional information
contains no prosthetic group
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O2
the enzyme requires dithiothreitol as a reducing agent and an oxygen free microenvironment (less than 1% (v/v)) for the dehydration of linalool
Ti(III)citrate
1 mM, complete inhibition
additional information
not inhibited by 10% (v/v) DMSO. EDTA (5 mM) does not affect the enzyme activity
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dithiothreitol
the aerobically purified enzyme is anaerobically activated in the presence of 2 mM dithiothreitol
S-adenosyl-L-methionine
40 mM, 2fold activation
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
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0.5
geraniol
pH 9.0, 35°C
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UniProt
brenda
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UniProt
brenda
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LDI_CASDE
397
0
44454
Swiss-Prot
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40000
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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proteolytic modification
precursor protein with a signal peptide for a periplasmic location
proteolytic modification
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precursor protein with a signal peptide for a periplasmic location
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expression in Escherichia coli
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Brodkorb, D.; Gottschall, M.; Marmulla, R.; Lüddeke, 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)
brenda
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5.4.4.4 geraniol isomerase
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