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Information on EC 1.1.1.347 - geraniol dehydrogenase (NAD+)
for references in articles please use BRENDA:EC1.1.1.347
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
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 .
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
showSynonyms
GeDH, geoA, geraniol DH, more
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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
MetaCyc
beta myrcene degradation, geraniol and nerol degradation
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesol + NAD+
(2E,6E)-farnesyl aldehyde + NADH + H+
-
Substrates: 50% activity compared to geraniol
Products: -
Products: -
?
(S)-perillyl alcohol + NAD+
? + NADH + H+
Substrates: most efficient substrate
Products: -
Products: -
?
(S)-perillyl alcohol + NAD+
perillyl aldehyde + NADH
Substrates: -
Products: -
Products: -
?
3-methyl-2-buten-1-ol + NAD+
3-methyl-but-2-enal + NADH + H+
-
Substrates: 4.3% activity compared to geraniol
Products: -
Products: -
?
geraniol + dichlorophenolindophenol
?
Substrates: -
Products: -
Products: -
?
geraniol + oxidized dichlorophenolindophenol
geranial + reduced dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
p-cumic alcohol + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
?
benzyl alcohol + NAD+
benzaldehyde + NADH + H+
Substrates: -
Products: -
Products: -
?
benzyl alcohol + NAD+
benzaldehyde + NADH + H+
Substrates: -
Products: -
Products: -
?
citronellol + NAD+
citronellal + NADH + H+
-
Substrates: 4.3% activity compared to geraniol
Products: -
Products: -
?
citronellol + NAD+
citronellal + NADH + H+
Substrates: -
Products: -
Products: -
?
geraniol + NAD+
geranial + NADH + H+
-
Substrates: the enzyme selectively oxidizes geraniol
Products: -
Products: -
ir
geraniol + NAD+
geranial + NADH + H+
Substrates: -
Products: -
Products: -
?
geraniol + NAD+
geranial + NADH + H+
Substrates: -
Products: -
Products: -
?
nerol + NAD+
neral + NADH + H+
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme cannot use phenazine methosulfate as alternative acceptor
Products: -
Products: -
?
additional information
?
-
Substrates: phenazine methosulfate is not accepted as an electron acceptor
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme cannot use phenazine methosulfate as alternative acceptor
Products: -
Products: -
?
additional information
?
-
Substrates: phenazine methosulfate is not accepted as an electron acceptor
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
geraniol + NAD+
geranial + NADH + H+
-
Substrates: the enzyme selectively oxidizes geraniol
Products: -
Products: -
ir
geraniol + NAD+
geranial + NADH + H+
Substrates: -
Products: -
Products: -
?
geraniol + NAD+
geranial + NADH + H+
Substrates: -
Products: -
Products: -
?
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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 21Ā°C
0.007
(S)-perillyl alcohol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
0.1157
benzyl alcohol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
0.17
benzyl alcohol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
0.0575
citronellol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
0.086
citronellol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
0.006
cumic alcohol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
0.021
cumic alcohol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
0.0033
geraniol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
0.05
geraniol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
0.0232
nerol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
0.045
nerol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°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
2020
(S)-perillyl alcohol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
3550
(S)-perillyl alcohol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
110
benzyl alcohol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
220
benzyl alcohol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
50
citronellol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
100
citronellol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
520
cumic alcohol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
940
cumic alcohol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
620
geraniol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
1570
geraniol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
310
nerol
native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°C
310
nerol
recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21Ā°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 21Ā°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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GEDH_CARLC
378
0
40630
Swiss-Prot
other Location (Reliability: 5)
ADH2_TANCI
379
0
41397
Swiss-Prot
other Location (Reliability: 3)
A3KI51_STRA7
Streptomyces ambofaciens (strain ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL B-2516)
368
2
38255
TrEMBL
-
A0A1V4XST1_9DELT
75
0
8521
TrEMBL
-
A0A1V5EDA2_9DELT
75
0
8521
TrEMBL
-
A0A084FZJ5_PSEDA
342
0
36497
TrEMBL
other Location (Reliability: 2)
A0A0M2H8A0_9MICO
534
0
55492
TrEMBL
-
A0A645IZ68_9ZZZZ
65
0
7108
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38272
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
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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
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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
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
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
EXTERNAL LINKS (specific for EC-Number 1.1.1.347)
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Release 2023.1 (January 2023)
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