Information on EC 1.2.1.94 - farnesal dehydrogenase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.2.1.94
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RECOMMENDED NAME
GeneOntology No.
farnesal dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesal + NAD+ + H2O = (2E,6E)-farnesoate + NADH + 2 H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
juvenile hormone III biosynthesis II
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juvenile hormone III biosynthesis I
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SYSTEMATIC NAME
IUBMB Comments
farnesal:NAD+ oxidoreductase
Invoved in juvenile hormone production in insects. The enzyme was described from the corpora allata of Drosophila melanogaster (fruit fly), Manduca sexta (tobacco hornworm) and Aedes aegypti (dengue mosquito).
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; Dengue mosquito
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Manually annotated by BRENDA team
Dengue mosquito
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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in the juvenile hormone JH III biosynthesis in insects, the alcohol farnesol, generated by the removal of diphosphate from farnesyl diphosphate, undergoes oxidation to the aldehyde (farnesal) and then to the acid (farnesoic acid). These steps are catalyzed by one or two NAD+-dependent dehydrogenase(s), JH III biosynthesis pathway, overview
physiological function
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesal + NAD+
(2E,6E)-farnesoate + NADH + 2 H+
show the reaction diagram
(2E,6E)-farnesal + NAD+ + H2O
(2E,6E)-farnesoate + NADH + 2 H+
show the reaction diagram
(2E,6E)-farnesal + NAD+ + H2O
(2E,6E)-farnesoic acid + NADH + H+
show the reaction diagram
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?
alpha-methyl-cinnamaldehyde + NAD+ + H2O
alpha-methyl-cinnamic acid + NADH + 2 H+
show the reaction diagram
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31% of the activity with farnesal
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?
citral + NAD+ + H2O
3,7-dimethyl-2,6-octadienoate + NADH + 2 H+
show the reaction diagram
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27% of the activity with farnesal
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?
decanal + NAD+ + H2O
decanoic acid + NADH + H+
show the reaction diagram
octanal + NAD+
octanoic acid + NADH
show the reaction diagram
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reaction products analyzed by LC-MS and identified based on the diagnostic ions
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?
octanal + NAD+ + H2O
octanoic acid + NADH + H+
show the reaction diagram
trans-cinnamaldehyde + NAD+ + H2O
trans-cinnamic acid + NADH + 2 H+
show the reaction diagram
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33% of the activity with farnesal
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesal + NAD+
(2E,6E)-farnesoate + NADH + 2 H+
show the reaction diagram
(2E,6E)-farnesal + NAD+ + H2O
(2E,6E)-farnesoate + NADH + 2 H+
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no activity with NADP+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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0.1 mM, 15% residual activity
4-chloromercuribenzoate
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0.1 mM, 21% residual activity
Ag+
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0.1 mM, no residual activity
Ca2+
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0.1 mM, 2% residual activity
Cu2+
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0.1 mM, no residual activity
Fe3+
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0.1 mM, 15% residual activity
iodoacetamide
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0.1 mM, 32% residual activity
Li+
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0.1 mM, 26% residual activity
Sodium azide
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0.1 mM, 20% residual activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
farnesal
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massive accumulation of the potentially toxic farnesal can stimulate the activity of a farnesal reductase or another enzyme that could convert farnesal back into farnesol
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13
(2E,6E)-farnesal
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pH 9.5, 35°C
1.28
alpha-methyl-cinnamaldehyde
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pH 9.5, 35°C
0.69
citral
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pH 9.5, 35°C
0.31
NAD+
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pH 9.5, 35°C
0.86
trans-cinnamaldehyde
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pH 9.5, 35°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.08
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recombinant AaALDH3-1-PB with farnesal and NADP+ as substrate, pH 9.5 and 37°C
7.13
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recombinant AaALDH3-1-PC with farnesal and NADP+ as substrate, pH 9.5 and 37°C
103.7
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recombinant AaALDH3-1-PD with decanal as substrate, pH 9.5 and 37°C
116.8
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recombinant AaALDH3-1-PB with octanal as substrate, pH 9.5 and 37°C
132.5
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recombinant AaALDH3-2 with decanal as substrate, pH 9.5 and 37°C
152.7
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recombinant AaALDH3-1-PA with octanal as substrate, pH 9.5 and 37°C
168.1
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recombinant AaALDH3-1-PD with octanal as substrate, pH 9.5 and 37°C
203.9
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recombinant AaALDH3-2 with octanal as substrate, pH 9.5 and 37°C
209.2
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recombinant AaALDH3-2 with farnesal as substrate, pH 9.5 and 37°C
214.6
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recombinant AaALDH3-1-PC with octanal as substrate, pH 9.5 and 37°C
268
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recombinant AaALDH3-1-PD with farnesal as substrate, pH 9.5 and 37°C
269.1
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recombinant AaALDH3-1-PB with farnesal as substrate, pH 9.5 and 37°C
272.9
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recombinant AaALDH3-1-PA with farnesal as substrate, pH 9.5 and 37°C
287.1
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recombinant AaALDH3-1-PB with decanal as substrate, pH 9.5 and 37°C
362.4
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recombinant AaALDH3-1-PC with decanal as substrate, pH 9.5 and 37°C
468.2
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recombinant AaALDH3-1-PC with farnesal as substrate, pH 9.5 and 37°C
additional information
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no activity of AaALDH3-1-PA with decanal, no activity of AaALDH3-1-PA, AaALDH3-1-PD, and AaALDH3-2 with NADP+
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
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rapid inactivation above
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
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isoelectric focusing
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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AaALDH3-1-RC transcript abundance, quantified by qPCR
Manually annotated by BRENDA team
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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the enzyme is found in all fractions of the cell
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Manually annotated by BRENDA team
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 70000, SDS-PAGE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli; five recombinant His-tagged AaALDH3s, representing AaALDH3-2 and the 4 splice variants of AaALDH3-1, PA, PB, PC, PD, overexpressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in the presence of an excess of farnesal and NAD+, highly active glands produces 10 times more farnesoic acid than suppressed glands, 24 h after blood feeding
injection of dsRNAs resulted in a approx. 80% significant reduction of AaALDH3-1 and AaALDH3-2 mRNAs, treatment with dsRNA for the AaALDH3-1 gene results in stronger reductions of farnesoic acid and juvenile hormone than treatment with dsRNA for the AaALDH3-2 gene
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.94)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)