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Information on EC 1.2.1.86 - geranial dehydrogenase
for references in articles please use BRENDA:EC1.2.1.86
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EC Tree 1 Oxidoreductases
1.2 Acting on the aldehyde or oxo group of donors
1.2.1 With NAD+ or NADP+ as acceptor
1.2.1.86 geranial dehydrogenase
IUBMB Comments
Does not act on neral.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
showSynonyms
geranial dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GADH
geoB
NAD+-dependent citral dehydrogenase
GADH
-
-
-
-
geoB
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranial + H2O + NAD+ = geranate + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
beta myrcene degradation, geraniol and nerol degradation
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SYSTEMATIC NAME
IUBMB Comments
geranial:NAD+ oxidoreductase
Does not act on neral.
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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
alpha-methyl cinnamaldehyde + NAD+ + H2O
alpha-methyl cinnamic acid + NADH + H+
-
Substrates: isoform citral dehydrogenase I shows 62% activity compared to citral, isoform citral dehydrogenase II shows 85% activity compared to citral
Products: -
Products: -
?
geranial + NAD+ + H2O
geranic acid + NADH + H+
-
Substrates: -
Products: -
Products: -
?
S-perillyl aldehyde + NAD+ + H2O
perillic acid + NADH + H+
-
Substrates: isoform citral dehydrogenase I shows 37% activity compared to citral, isoform citral dehydrogenase II shows 54% activity compared to citral
Products: -
Products: -
?
trans-cinnamaldehyde + NAD+ + H2O
cinnamic acid + NADH + H+
-
Substrates: isoform citral dehydrogenase I shows 73% activity compared to citral, isoform citral dehydrogenase II shows 87% activity compared to citral
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows no reaction with NADP+. No reduction reaction is observed either with NADH or NADPH as a coenzyme
Products: -
Products: -
-
citral + NAD+ + H2O
geranic acid + NADH + H+
-
Substrates: 100% activity
Products: -
Products: -
ir
geranial + H2O + NAD+
geranate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
geranial + H2O + NAD+
geranate + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
geranial + H2O + NAD+
geranate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
geranial + H2O + NAD+
geranate + NADH + H+
-
Substrates: geranial is partially transformed into geranic acid by NAD+-dependent citral dehydrogenase activity
Products: -
Products: -
?
geranial + H2O + NAD+
geranate + NADH + H+
-
Substrates: geranial is partially transformed into geranic acid by NAD+-dependent citral dehydrogenase activity
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme activity is independent of coenzyme A
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.11
alpha-methyl cinnamaldehyde
-
isoform citral dehydrogenase I, at pH 9.5 and 35°C
1.54
alpha-methyl cinnamaldehyde
-
isoform citral dehydrogenase II, at pH 9.5 and 35°C
2.5
S-perillyl aldehyde
-
isoform citral dehydrogenase II, at pH 9.5 and 35°C
-
3.33
S-perillyl aldehyde
-
isoform citral dehydrogenase I, at pH 9.5 and 35°C
-
0.83
trans-cinnamaldehyde
-
isoform citral dehydrogenase I, at pH 9.5 and 35°C
1.25
trans-cinnamaldehyde
-
isoform citral dehydrogenase II, at pH 9.5 and 35°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
138
-
isoform citral dehydrogenase II, after 31.5fold purification, at pH 9.5and 35°C
241.2
-
isoform citral dehydrogenase I, after 54.9fold purification, at pH 9.5 and 35°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 11
-
below pH 8.0, both isoenzymes show less than 50% of relative activity while complete inactivation is observed at pH 5.0-6.0 and pH 10.5-11.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
metabolism
metabolism
-
the enzyme contributes to the formation of geranic acid
metabolism
-
the enzyme contributes to the formation of geranic acid
-
Show AA Sequence and Transmembrane Helices (196 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
heterodimer
-
1 * 62000 + 1 * 60000, isoform citral dehydrogenase I, SDS-PAGE
heterodimer
-
1 * 65000 + 1 * 58000, isoform citral dehydrogenase II, SDS-PAGE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
20% of citral dehydrogenase II activity remains while citral dehydrogenase I is completely inactivated at 60°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Toyopearl GigaCapQ-650 M column chromatography, Toyopearl Giga Cap S-650 M column chromatography, Toyopearl AF-Blue-650 M column chromatography and TSK gel G3000SW gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
brenda
Wolken, W.; Van Der Werf, M.
Geraniol biotransformation-pathway in spores of Penicillium digitatum
Appl. Microbiol. Biotechnol.
57
731-737
2001
Penicillium digitatum, Penicillium digitatum ATCC 201167
brenda
Lueddeke, F.; Dikfidan, A.; Harder, J.
Physiology of deletion mutants in the anaerobic beta-myrcene degradation pathway in Castellaniella defragrans
BMC Microbiol.
12
192
2012
Castellaniella defragrans, Castellaniella defragrans 65Phen
brenda
Nik-Abdul-Ghani, N.; Mohamed-Hussein, Z.; Hassan, M.
Citral dehydrogenase involved in geraniol oxidation pathway purification, characterization and kinetic studies from Persicaria minor (Polygonum minus Huds.)
J. Plant Biochem. Biotechnol.
27
1-12
2018
Persicaria minor
-
brenda
EXTERNAL LINKS (specific for EC-Number 1.2.1.86)
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Release 2023.1 (January 2023)
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