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Enzyme Nomenclature
Information on EC 1.1.1.347 - geraniol dehydrogenase (NAD+)
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.1.1.347
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RECOMMENDED NAME
GeneOntology No.
geraniol dehydrogenase (NAD+)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geraniol + NAD+ = geranial + NADH + H+
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
geraniol:NAD+ oxidoreductase
The enzyme from the bacterium Castellaniella defragrans is most active in vitro with perillyl alcohol [2]. The enzyme from the prune mite Carpoglyphus lactis also acts (more slowly) on farnesol but not on nerol [1].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the enzyme plays an important role in the biosynthesis of neral, an alarm pheromone in Carpoglyphus lactis
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesol + NAD+
(2E,6E)-farnesyl aldehyde + NADH + H+
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50% activity compared to geraniol
-
-
?
(S)-perillyl alcohol + NAD+
perillyl aldehyde + NADH
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-
-
?
3-methyl-2-buten-1-ol + NAD+
3-methyl-but-2-enal + NADH + H+
-
4.3% activity compared to geraniol
-
-
?
geraniol + oxidized dichlorophenolindophenol
geranial + reduced dichlorophenolindophenol
-
-
-
?
(S)-perillyl alcohol + NAD+
? + NADH + H+
most efficient substrate
-
-
?
(S)-perillyl alcohol + NAD+
? + NADH + H+
most efficient substrate
-
-
?
benzyl alcohol + NAD+
benzaldehyde + NADH + H+
-
-
-
?
citronellol + NAD+
citronellal + NADH + H+
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4.3% activity compared to geraniol
-
-
?
geraniol + NAD+
geranial + NADH + H+
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the enzyme selectively oxidizes geraniol
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-
ir
additional information
?
-
-
NADP+ is ineffective as a cofactor. The enzyme does not use nerol as substrate. Straight-chain alcohols such as 1-octanol, 2-buten-1-ol, 1-butanol and ethanol serve as poor substrates
-
-
-
additional information
?
-
the enzyme cannot use phenazine methosulfate as alternative acceptor
-
-
-
additional information
?
-
phenazine methosulfate is not accepted as an electron acceptor
-
-
-
additional information
?
-
the enzyme cannot use phenazine methosulfate as alternative acceptor
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-
-
additional information
?
-
phenazine methosulfate is not accepted as an electron acceptor
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
geraniol + NAD+
geranial + NADH + H+
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the enzyme selectively oxidizes geraniol
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-
ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
enzyme reduces one molecule of NAD+ to NADH per geraniol molecule provided
additional information
NADPH is ineffective as a cosubstrate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-cyclohexyl-N-(2-morpholinoethyl)carbodiimide
I80 of less than 34 mM
EDTA
7 mM, 96% inhibition; 7 mM EDTA inhibits the enzyme by 96%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0044
(S)-perillyl alcohol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
0.007
(S)-perillyl alcohol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C; pH 9.4, 21°C
0.1157
benzyl alcohol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
0.17
benzyl alcohol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C; pH 9.4, 21°C
0.0575
citronellol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
0.086
citronellol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C; pH 9.4, 21°C
0.006
cumic alcohol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
0.021
cumic alcohol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
0.0033
geraniol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
0.05
geraniol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
0.0232
nerol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
0.045
nerol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C; pH 9.4, 21°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
310
nerol
Castellaniella defragrans
H1ZV38
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C; pH 9.4, 21°C; recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
2280
2020
(S)-perillyl alcohol
Castellaniella defragrans
H1ZV38
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C; pH 9.4, 21°C
13242
3550
(S)-perillyl alcohol
Castellaniella defragrans
H1ZV38
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
13242
110
benzyl alcohol
Castellaniella defragrans
H1ZV38
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
260
220
benzyl alcohol
Castellaniella defragrans
H1ZV38
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C; pH 9.4, 21°C
260
50
citronellol
Castellaniella defragrans
H1ZV38
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
4512
100
citronellol
Castellaniella defragrans
H1ZV38
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C; pH 9.4, 21°C
4512
520
cumic alcohol
Castellaniella defragrans
H1ZV38
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
42407
940
cumic alcohol
Castellaniella defragrans
H1ZV38
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
42407
620
geraniol
Castellaniella defragrans
H1ZV38
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
987
1570
geraniol
Castellaniella defragrans
H1ZV38
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C; pH 9.4, 21°C
987
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the crude cell extract shows a specific activity of 0.056 units/mg, while the 114fold purified enzyme shows a specific activity of 4.33 units/mg at pH 9.4 and 21°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
-
as the pH increases from 7.0 to 7.5, there is a sharp increase in enzyme activity whereas the activity decreases sharply beyond pH 10.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38272
2 * 38272, calculated; 2 * 38272, calculated from amino acid sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
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1 * 40630, calculated from amino acid sequence; 1 * 42800, active form, SDS-PAGE
homodimer
2 * 38272, calculated from amino acid sequence; 2 * 39000, SDS-PAGE
homodimer
-
2 * 38272, calculated from amino acid sequence; 2 * 39000, SDS-PAGE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Toyopearl phenyl-650M column chromatography, Toyopearl HW-50F column chromatography, DEAE-cellulose column chromatography, Blue-Cellulofine column chromatography, MonoQ column chromatography and Superdex 200gel filtration
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DEAE column chromatography and phenyl-Sepharose 6 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21 Star(DE3); expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activitiy is induced during growth with limonene in comparison to growth with acetate; enzyme activity is induced during growth with limonene in comparison to growth with acetate
activitiy is induced during growth with limonene in comparison to growth with acetate; enzyme activity is induced during growth with limonene in comparison to growth with acetate
activitiy is induced during growth with limonene in comparison to growth with acetate; enzyme activity is induced during growth with limonene in comparison to growth with acetate
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.347)
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