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Enzyme Nomenclature
Information on EC 1.1.1.347 - geraniol dehydrogenase (NAD+)
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1.1.1.347 geraniol dehydrogenase (NAD+)IUBMB Comments
The enzyme from the bacterium Castellaniella defragrans is most active in vitro with perillyl alcohol . The enzyme from the prune mite Carpoglyphus lactis also acts (more slowly) on farnesol but not on nerol .
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GeDH
geoA
geraniol DH
GeDH
-
-
-
-
geoA
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geraniol + NAD+ = geranial + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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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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+
-
50% activity compared to geraniol
-
-
?
(S)-perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
-
-
?
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+
-
4.3% activity compared to geraniol
-
-
?
geraniol + NAD+
geranial + NADH + H+
-
the enzyme selectively oxidizes geraniol
-
-
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
-
-
-
additional information
?
-
phenazine methosulfate is not accepted as an electron acceptor
-
-
-
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NATURAL SUBSTRATE
NATURAL 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
geraniol + NAD+
geranial + NADH + H+
-
the enzyme selectively oxidizes geraniol
-
-
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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INHIBITOR
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
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
2020
(S)-perillyl alcohol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C; pH 9.4, 21°C
3550
(S)-perillyl alcohol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
110
benzyl alcohol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
220
benzyl alcohol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C; pH 9.4, 21°C
50
citronellol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
100
citronellol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C; pH 9.4, 21°C
520
cumic alcohol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
940
cumic alcohol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
620
geraniol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C
1570
geraniol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C; pH 9.4, 21°C
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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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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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
A0A1V4XST1_9DELT
75
0
8521
TrEMBL
A3KI51_STRA7
Streptomyces ambofaciens (strain ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL B-2516)
368
2
38255
TrEMBL
A0A0M2H8A0_9MICO
534
0
55492
TrEMBL
A0A1V5EDA2_9DELT
75
0
8521
TrEMBL
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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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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
-
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
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Noge, K.; Kato, M.; Mori, N.; Kataoka, M.; Tanaka, C.; Yamasue, Y.; Nishida, R.; Kuwahara, Y.
Geraniol dehydrogenase, the key enzyme in biosynthesis of the alarm pheromone, from the astigmatid mite Carpoglyphus lactis (Acari: Carpoglyphidae)
FEBS J.
275
2807-2817
2008
Carpoglyphus lactis
brenda
Lueddeke, F.; Wuelfing, A.; Timke, M.; Germer, F.; Weber, J.; Dikfidan, A.; Rahnfeld, T.; Linder, D.; Meyerdierks, A.; Harder, J.
Geraniol and geranial dehydrogenases induced in anaerobic monoterpene degradation by Castellaniella defragrans
Appl. Environ. Microbiol.
78
2128-2136
2012
Castellaniella defragrans (H1ZV38), Castellaniella defragrans 65Phen (H1ZV38)
brenda
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