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Information on EC 5.4.4.4 - geraniol isomerase and Organism(s) Castellaniella defragrans and UniProt Accession E1XUJ2

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EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.4 Transferring hydroxy groups
                5.4.4.4 geraniol isomerase
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.
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This record set is specific for:
Castellaniella defragrans
UNIPROT: E1XUJ2
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The taxonomic range for the selected organisms is: Castellaniella defragrans
The expected taxonomic range for this enzyme is: Castellaniella defragrans
Reaction Schemes
Synonyms
geraniol isomerase, more
SYSTEMATIC NAME
IUBMB Comments
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
geraniol
linalool
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
geraniol
linalool
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
contains no prosthetic group
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
geraniol
pH 9.0, 35°C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LDI_CASDE
397
0
44454
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
gel filtration
40000
4 * 40000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 40000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
precursor protein with a signal peptide for a periplasmic location
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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)
Manually annotated by BRENDA team