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Information on EC 1.2.1.94 - farnesal dehydrogenase
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1.2.1.94 farnesal dehydrogenaseIUBMB Comments
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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Word Map
- 1.2.1.94
-
corneal
-
polycyclic
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farnesoic
- 2,3,7,8-tetrachlorodibenzo-p-dioxin
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blat
- aldh3b1
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clusterin
- allata
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granulosa-lutein
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as-odn
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opossum
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endometriosis
The enzyme appears in viruses and cellular organisms
Synonyms
aldehyde dehydrogenase 3, aaaldh3, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AaALDH3
AaALDH3-1
AaALDH3-2
AaeL_AAEL012161
AaeL_AAEL012162
AaeL_AAEL012165
aldehyde dehydrogenase 3
ALDH3
NAD+-dependent class 3 ALDH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesal + NAD+ + H2O = (2E,6E)-farnesoate + NADH + 2 H+
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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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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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
alpha-methyl-cinnamaldehyde + NAD+ + H2O
alpha-methyl-cinnamic acid + NADH + 2 H+
-
31% of the activity with farnesal
-
-
?
citral + NAD+ + H2O
3,7-dimethyl-2,6-octadienoate + NADH + 2 H+
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27% of the activity with farnesal
-
-
?
octanal + NAD+
octanoic acid + NADH
-
-
reaction products analyzed by LC-MS and identified based on the diagnostic ions
-
?
trans-cinnamaldehyde + NAD+ + H2O
trans-cinnamic acid + NADH + 2 H+
-
33% of the activity with farnesal
-
-
?
(2E,6E)-farnesal + NAD+
(2E,6E)-farnesoate + NADH + 2 H+
-
NADP+ can not substitute NAD+, AaALDH3-1-PC has the highest activity with farnesal, AaALDH3-1 is mainly responsible for the conversion of farnesal to farnesoic acid
reaction products analyzed by LC-MS and identified based on the diagnostic ions
-
?
(2E,6E)-farnesal + NAD+
(2E,6E)-farnesoate + NADH + 2 H+
-
NADP+ can not substitute NAD+, AaALDH3-1-PC has the highest activity with farnesal, AaALDH3-1 is mainly responsible for the conversion of farnesal to farnesoic acid
reaction products analyzed by LC-MS and identified based on the diagnostic ions
-
?
(2E,6E)-farnesal + NAD+ + H2O
(2E,6E)-farnesoate + NADH + 2 H+
-
substrate specificity for the 2E-isomer
-
-
?
(2E,6E)-farnesal + NAD+ + H2O
(2E,6E)-farnesoic acid + NADH + 2 H+
-
-
-
?
(2E,6E)-farnesal + NAD+ + H2O
(2E,6E)-farnesoic acid + NADH + 2 H+
-
-
-
?
decanal + NAD+ + H2O
decanoic acid + NADH + 2 H+
-
-
-
?
decanal + NAD+ + H2O
decanoic acid + NADH + H+
-
-
reaction products analyzed by LC-MS and identified based on the diagnostic ions
-
?
decanal + NAD+ + H2O
decanoic acid + NADH + H+
-
-
reaction products analyzed by LC-MS and identified based on the diagnostic ions
-
?
octanal + NAD+ + H2O
octanoic acid + NADH + 2 H+
-
-
-
?
additional information
?
-
Q16MV5
AaALDH3s oxidizes farnesal to FA in the presence of NAD+, and NADP+ cannot substitute for NAD+. AaALDH3-1-PC has the highest activity with farnesal. All of the AaALDH3-1 enzyme splice variants oxidize octanal and decanal with the exception of AaALDH3-1-PA which does not have activity with decanal
-
-
-
additional information
?
-
AaALDH3s oxidizes farnesal to FA in the presence of NAD+, and NADP+ cannot substitute for NAD+. AaALDH3-1-PC has the highest activity with farnesal. All of the AaALDH3-1 enzyme splice variants oxidize octanal and decanal with the exception of AaALDH3-1-PA which does not have activity with decanal
-
-
-
additional information
?
-
AaALDH3s oxidizes farnesal to FA in the presence of NAD+, and NADP+ cannot substitute for NAD+. AaALDH3-1-PC has the highest activity with farnesal. All of the AaALDH3-1 enzyme splice variants oxidize octanal and decanal with the exception of AaALDH3-1-PA which does not have activity with decanal
-
-
-
additional information
?
-
Q16MV5
AaALDH3s oxidizes farnesal to FA in the presence of NAD+, and NADP+ cannot substitute for NAD+. AaALDH3-1-PC has the highest activity with farnesal. All of the AaALDH3-1 enzyme splice variants oxidize octanal and decanal with the exception of AaALDH3-1-PA which does not have activity with decanal
-
-
-
additional information
?
-
AaALDH3s oxidizes farnesal to FA in the presence of NAD+, and NADP+ cannot substitute for NAD+. AaALDH3-1-PC has the highest activity with farnesal. All of the AaALDH3-1 enzyme splice variants oxidize octanal and decanal with the exception of AaALDH3-1-PA which does not have activity with decanal
-
-
-
additional information
?
-
AaALDH3s oxidizes farnesal to FA in the presence of NAD+, and NADP+ cannot substitute for NAD+. AaALDH3-1-PC has the highest activity with farnesal. All of the AaALDH3-1 enzyme splice variants oxidize octanal and decanal with the exception of AaALDH3-1-PA which does not have activity with decanal
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-
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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
(2E,6E)-farnesal + NAD+
(2E,6E)-farnesoate + NADH + 2 H+
-
NADP+ can not substitute NAD+, AaALDH3-1-PC has the highest activity with farnesal, AaALDH3-1 is mainly responsible for the conversion of farnesal to farnesoic acid
reaction products analyzed by LC-MS and identified based on the diagnostic ions
-
?
(2E,6E)-farnesal + NAD+
(2E,6E)-farnesoate + NADH + 2 H+
-
NADP+ can not substitute NAD+, AaALDH3-1-PC has the highest activity with farnesal, AaALDH3-1 is mainly responsible for the conversion of farnesal to farnesoic acid
reaction products analyzed by LC-MS and identified based on the diagnostic ions
-
?
(2E,6E)-farnesal + NAD+ + H2O
(2E,6E)-farnesoate + NADH + 2 H+
-
substrate specificity for the 2E-isomer
-
-
?
(2E,6E)-farnesal + NAD+ + H2O
(2E,6E)-farnesoic acid + NADH + 2 H+
Q16MV5, Q16MV6, Q16MV7
-
-
-
?
(2E,6E)-farnesal + NAD+ + H2O
(2E,6E)-farnesoic acid + NADH + 2 H+
Q16MV5, Q16MV6, Q16MV7
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Q16MV5
AaALDH3s oxidizes farnesal to FA in the presence of NAD+, and NADP+ cannot substitute for NAD+
-
additional information
AaALDH3s oxidizes farnesal to FA in the presence of NAD+, and NADP+ cannot substitute for NAD+
-
additional information
AaALDH3s oxidizes farnesal to FA in the presence of NAD+, and NADP+ cannot substitute for NAD+
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
farnesal
-
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
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.08
-
recombinant AaALDH3-1-PB with farnesal and NADP+ as substrate, pH 9.5 and 37°C
7.13
-
recombinant AaALDH3-1-PC with farnesal and NADP+ as substrate, pH 9.5 and 37°C
additional information
-
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
LITERATURE
9.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
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
additional information
AaALDH3 enzyme activity, as well as the concentrations of farnesol, farnesal and farnesoic acid are different in corporae allatae of sugar and blood-fed females; AaALDH3 enzyme activity, as well as the concentrations of farnesol, farnesal and farnesoic acid are different in corporae allatae of sugar and blood-fed females; AaALDH3 enzyme activity, as well as the concentrations of farnesol, farnesal and farnesoic acid are different in corporae allatae of sugar and blood-fed females
brenda
-
AaALDH3 enzyme activity, as well as the concentrations of farnesol, farnesal and farnesoic acid are different in corporae allatae of sugar and blood-fed females; AaALDH3 enzyme activity, as well as the concentrations of farnesol, farnesal and farnesoic acid are different in corporae allatae of sugar and blood-fed females; AaALDH3 enzyme activity, as well as the concentrations of farnesol, farnesal and farnesoic acid are different in corporae allatae of sugar and blood-fed females
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brenda
-
presents the five transcripts, with their relative proportions changing during development
brenda
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presents the five transcripts, with their relative proportions changing during development
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brenda
-
AaALDH3-1-RB transcript abundance, quantified by qPCR
brenda
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AaALDH3-1-RB transcript abundance, quantified by qPCR
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brenda
-
AaALDH3-1-RD transcript abundance, quantified by qPCR
-
brenda
additional information
-
AaALDH3-2 gene has comparatively lower levels of transcript
brenda
additional information
Q16MV5
the enzyme shows tissue and developmental-stage-specific splice variants; the enzyme shows tissue and developmental-stage-specific splice variants, determination of transcript abundance for the AaALDH3 genes, including the splice variants (RA, RB, RC and RD), quantified by quantitative PCR; the enzyme shows tissue and developmental-stage-specific splice variants, determination of transcript abundance for the AaALDH3 genes quantified by quantitative PCR
brenda
additional information
the enzyme shows tissue and developmental-stage-specific splice variants; the enzyme shows tissue and developmental-stage-specific splice variants, determination of transcript abundance for the AaALDH3 genes, including the splice variants (RA, RB, RC and RD), quantified by quantitative PCR; the enzyme shows tissue and developmental-stage-specific splice variants, determination of transcript abundance for the AaALDH3 genes quantified by quantitative PCR
brenda
additional information
the enzyme shows tissue and developmental-stage-specific splice variants; the enzyme shows tissue and developmental-stage-specific splice variants, determination of transcript abundance for the AaALDH3 genes, including the splice variants (RA, RB, RC and RD), quantified by quantitative PCR; the enzyme shows tissue and developmental-stage-specific splice variants, determination of transcript abundance for the AaALDH3 genes quantified by quantitative PCR
brenda
additional information
-
AaALDH3-2 gene has comparatively lower levels of transcript; the enzyme shows tissue and developmental-stage-specific splice variants; the enzyme shows tissue and developmental-stage-specific splice variants, determination of transcript abundance for the AaALDH3 genes, including the splice variants (RA, RB, RC and RD), quantified by quantitative PCR; the enzyme shows tissue and developmental-stage-specific splice variants, determination of transcript abundance for the AaALDH3 genes quantified by quantitative PCR
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the enzyme is found in all fractions of the cell
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
the enzyme is a member of the NAD+-dependent class 3 ALDH family of the aldehyde dehydrogenase superfamily; the enzyme is a member of the NAD+-dependent class 3 ALDH family of the aldehyde dehydrogenase superfamily; the enzyme is a member of the NAD+-dependent class 3 ALDH family of the aldehyde dehydrogenase superfamily
evolution
-
the enzyme is a member of the NAD+-dependent class 3 ALDH family of the aldehyde dehydrogenase superfamily; the enzyme is a member of the NAD+-dependent class 3 ALDH family of the aldehyde dehydrogenase superfamily; the enzyme is a member of the NAD+-dependent class 3 ALDH family of the aldehyde dehydrogenase superfamily
-
malfunction
reduction of AaALDH3 activity results in accumulation of farnesal and conversion back to farnesol that leaks outside the corpora allata; reduction of AaALDH3 activity results in accumulation of farnesal and conversion back to farnesol that leaks outside the corpora allata; reduction of AaALDH3 activity results in accumulation of farnesal and conversion back to farnesol that leaks outside the corpora allata
malfunction
-
reduction of AaALDH3 activity results in accumulation of farnesal and conversion back to farnesol that leaks outside the corpora allata; reduction of AaALDH3 activity results in accumulation of farnesal and conversion back to farnesol that leaks outside the corpora allata; reduction of AaALDH3 activity results in accumulation of farnesal and conversion back to farnesol that leaks outside the corpora allata
-
metabolism
-
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
metabolism
the enzyme is a biosynthetic enzyme of the juvenile hormone JH pathway; the enzyme is a biosynthetic enzyme of the juvenile hormone JH pathway; the enzyme is a biosynthetic enzyme of the juvenile hormone JH pathway
metabolism
-
the enzyme is a biosynthetic enzyme of the juvenile hormone JH pathway; the enzyme is a biosynthetic enzyme of the juvenile hormone JH pathway; the enzyme is a biosynthetic enzyme of the juvenile hormone JH pathway
-
physiological function
-
results suggest that in the female Dengue mosquito Aedes aegypti, AaALDH3 enzyme plays a critical role in the regulation of juvenile hormone biosynthesis after blood feeding; the enzyme plays a key role in the regulation of juvenile hormone synthesis in blood-fed mosquito females
physiological function
the enzyme is a fatty aldehyde dehydrogenase (AaALDH3), NAD+-dependent class 3 ALDH, that oxidizes farnesal into farnesoic acid in the corpora allata of mosquitoes. In corporae allatae of blood-fed females, the low catalytic activity of AaALDH3 limits the flux of precursors and causes a remarkable increase in the pool of farnesal with a decrease in farnesoic acid and juvenile hormone synthesis. The accumulation of the potentially toxic farnesal stimulates the activity of a reductase that converts farnesal back into farnesol, resulting in farnesol leaking out of the corpora allata. Enzyme AaALDH3 plays a key role in the regulation of juvenile hormone synthesis in blood-fed females and mosquitoes seem to have developed a trade-off system to balance the key role of farnesal as a juvenile hormone precursor with its potential toxicity; the enzyme is a fatty aldehyde dehydrogenase (AaALDH3), NAD+-dependent class 3 ALDH, that oxidizes farnesal into farnesoic acid in the corpora allata of mosquitoes. In corporae allatae of blood-fed females, the low catalytic activity of AaALDH3 limits the flux of precursors and causes a remarkable increase in the pool of farnesal with a decrease in farnesoic acid and juvenile hormone synthesis. The accumulation of the potentially toxic farnesal stimulates the activity of a reductase that converts farnesal back into farnesol, resulting in farnesol leaking out of the corpora allata. Enzyme AaALDH3 plays a key role in the regulation of juvenile hormone synthesis in blood-fed females and mosquitoes seem to have developed a trade-off system to balance the key role of farnesal as a juvenile hormone precursor with its potential toxicity; the enzyme is a fatty aldehyde dehydrogenase (AaALDH3), NAD+-dependent class 3 ALDH, that oxidizes farnesal into farnesoic acid in the corpora allata of mosquitoes. In corporae allatae of blood-fed females, the low catalytic activity of AaALDH3 limits the flux of precursors and causes a remarkable increase in the pool of farnesal with a decrease in farnesoic acid and juvenile hormone synthesis. The accumulation of the potentially toxic farnesal stimulates the activity of a reductase that converts farnesal back into farnesol, resulting in farnesol leaking out of the corpora allata. Enzyme AaALDH3 plays a key role in the regulation of juvenile hormone synthesis in blood-fed females and mosquitoes seem to have developed a trade-off system to balance the key role of farnesal as a juvenile hormone precursor with its potential toxicity
physiological function
-
results suggest that in the female Dengue mosquito Aedes aegypti, AaALDH3 enzyme plays a critical role in the regulation of juvenile hormone biosynthesis after blood feeding; the enzyme is a fatty aldehyde dehydrogenase (AaALDH3), NAD+-dependent class 3 ALDH, that oxidizes farnesal into farnesoic acid in the corpora allata of mosquitoes. In corporae allatae of blood-fed females, the low catalytic activity of AaALDH3 limits the flux of precursors and causes a remarkable increase in the pool of farnesal with a decrease in farnesoic acid and juvenile hormone synthesis. The accumulation of the potentially toxic farnesal stimulates the activity of a reductase that converts farnesal back into farnesol, resulting in farnesol leaking out of the corpora allata. Enzyme AaALDH3 plays a key role in the regulation of juvenile hormone synthesis in blood-fed females and mosquitoes seem to have developed a trade-off system to balance the key role of farnesal as a juvenile hormone precursor with its potential toxicity; the enzyme is a fatty aldehyde dehydrogenase (AaALDH3), NAD+-dependent class 3 ALDH, that oxidizes farnesal into farnesoic acid in the corpora allata of mosquitoes. In corporae allatae of blood-fed females, the low catalytic activity of AaALDH3 limits the flux of precursors and causes a remarkable increase in the pool of farnesal with a decrease in farnesoic acid and juvenile hormone synthesis. The accumulation of the potentially toxic farnesal stimulates the activity of a reductase that converts farnesal back into farnesol, resulting in farnesol leaking out of the corpora allata. Enzyme AaALDH3 plays a key role in the regulation of juvenile hormone synthesis in blood-fed females and mosquitoes seem to have developed a trade-off system to balance the key role of farnesal as a juvenile hormone precursor with its potential toxicity; the enzyme is a fatty aldehyde dehydrogenase (AaALDH3), NAD+-dependent class 3 ALDH, that oxidizes farnesal into farnesoic acid in the corpora allata of mosquitoes. In corporae allatae of blood-fed females, the low catalytic activity of AaALDH3 limits the flux of precursors and causes a remarkable increase in the pool of farnesal with a decrease in farnesoic acid and juvenile hormone synthesis. The accumulation of the potentially toxic farnesal stimulates the activity of a reductase that converts farnesal back into farnesol, resulting in farnesol leaking out of the corpora allata. Enzyme AaALDH3 plays a key role in the regulation of juvenile hormone synthesis in blood-fed females and mosquitoes seem to have developed a trade-off system to balance the key role of farnesal as a juvenile hormone precursor with its potential toxicity; the enzyme plays a key role in the regulation of juvenile hormone synthesis in blood-fed mosquito females
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Q16MV5
specific target sequences for dsRNA synthesis are designed for each splice variant of AaALDH3-1 by selecting regions in the splice variant-specific exons. dsRNA for AaALDH3-2 as well as dsRNA against a common region to all splice variants of AaALDH3-1 (AaALDH3-1-RA, AaALDH3-1-RB, AaALDH3-1-RC, AaALDH3-1-RD) are also designed. Specificity and efficiency of AaALDH3-1 dsRNAi, specificity of silencing the AaALDH3-1-RC variant, only AaALDH3-1-RC transcripts are depleted; target sequences for dsRNA synthesis are designed for each splice variant of AaALDH3-1 by selecting regions in the splice variant-specific exons. dsRNA for AaALDH3-2 as well as dsRNA against a common region to all splice variants of AaALDH3-1 (AaALDH3-1-RA, AaALDH3-1-RB, AaALDH3-1-RC, AaALDH3-1-RD) are also designed; target sequences for dsRNA synthesis are designed for each splice variant of AaALDH3-1 by selecting regions in the splice variant-specific exons. dsRNA for AaALDH3-2 as well as dsRNA against a common region to all splice variants of AaALDH3-1 (AaALDH3-1-RA, AaALDH3-1-RB, AaALDH3-1-RC, AaALDH3-1-RD) are also designed
additional information
specific target sequences for dsRNA synthesis are designed for each splice variant of AaALDH3-1 by selecting regions in the splice variant-specific exons. dsRNA for AaALDH3-2 as well as dsRNA against a common region to all splice variants of AaALDH3-1 (AaALDH3-1-RA, AaALDH3-1-RB, AaALDH3-1-RC, AaALDH3-1-RD) are also designed. Specificity and efficiency of AaALDH3-1 dsRNAi, specificity of silencing the AaALDH3-1-RC variant, only AaALDH3-1-RC transcripts are depleted; target sequences for dsRNA synthesis are designed for each splice variant of AaALDH3-1 by selecting regions in the splice variant-specific exons. dsRNA for AaALDH3-2 as well as dsRNA against a common region to all splice variants of AaALDH3-1 (AaALDH3-1-RA, AaALDH3-1-RB, AaALDH3-1-RC, AaALDH3-1-RD) are also designed; target sequences for dsRNA synthesis are designed for each splice variant of AaALDH3-1 by selecting regions in the splice variant-specific exons. dsRNA for AaALDH3-2 as well as dsRNA against a common region to all splice variants of AaALDH3-1 (AaALDH3-1-RA, AaALDH3-1-RB, AaALDH3-1-RC, AaALDH3-1-RD) are also designed
additional information
specific target sequences for dsRNA synthesis are designed for each splice variant of AaALDH3-1 by selecting regions in the splice variant-specific exons. dsRNA for AaALDH3-2 as well as dsRNA against a common region to all splice variants of AaALDH3-1 (AaALDH3-1-RA, AaALDH3-1-RB, AaALDH3-1-RC, AaALDH3-1-RD) are also designed. Specificity and efficiency of AaALDH3-1 dsRNAi, specificity of silencing the AaALDH3-1-RC variant, only AaALDH3-1-RC transcripts are depleted; target sequences for dsRNA synthesis are designed for each splice variant of AaALDH3-1 by selecting regions in the splice variant-specific exons. dsRNA for AaALDH3-2 as well as dsRNA against a common region to all splice variants of AaALDH3-1 (AaALDH3-1-RA, AaALDH3-1-RB, AaALDH3-1-RC, AaALDH3-1-RD) are also designed; target sequences for dsRNA synthesis are designed for each splice variant of AaALDH3-1 by selecting regions in the splice variant-specific exons. dsRNA for AaALDH3-2 as well as dsRNA against a common region to all splice variants of AaALDH3-1 (AaALDH3-1-RA, AaALDH3-1-RB, AaALDH3-1-RC, AaALDH3-1-RD) are also designed
additional information
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specific target sequences for dsRNA synthesis are designed for each splice variant of AaALDH3-1 by selecting regions in the splice variant-specific exons. dsRNA for AaALDH3-2 as well as dsRNA against a common region to all splice variants of AaALDH3-1 (AaALDH3-1-RA, AaALDH3-1-RB, AaALDH3-1-RC, AaALDH3-1-RD) are also designed. Specificity and efficiency of AaALDH3-1 dsRNAi, specificity of silencing the AaALDH3-1-RC variant, only AaALDH3-1-RC transcripts are depleted; target sequences for dsRNA synthesis are designed for each splice variant of AaALDH3-1 by selecting regions in the splice variant-specific exons. dsRNA for AaALDH3-2 as well as dsRNA against a common region to all splice variants of AaALDH3-1 (AaALDH3-1-RA, AaALDH3-1-RB, AaALDH3-1-RC, AaALDH3-1-RD) are also designed; target sequences for dsRNA synthesis are designed for each splice variant of AaALDH3-1 by selecting regions in the splice variant-specific exons. dsRNA for AaALDH3-2 as well as dsRNA against a common region to all splice variants of AaALDH3-1 (AaALDH3-1-RA, AaALDH3-1-RB, AaALDH3-1-RC, AaALDH3-1-RD) are also designed
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexane
hexane
enzyme inactivation at about 40% v/v hexane; enzyme inactivation at about 40% v/v hexane; enzyme inactivation at about 40% v/v hexane
hexane
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enzyme inactivation at about 40% v/v hexane; enzyme inactivation at about 40% v/v hexane; enzyme inactivation at about 40% v/v hexane
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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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gene AaALDH3-1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, the enzyme shows tissue and developmental-stage-specific splice variants, four splice variants of AaALDH3-1 (PA, PB, PC and PD), recombinant expression of His-tagged enzyme in Escherichia coli, quantitative real-time PCR enzyme expression analysis; gene AaALDH3-2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, the enzyme shows tissue and developmental-stage-specific splice variants; gene AaALDH3-2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, the enzyme shows tissue and developmental-stage-specific splice variants, determination of transcript abundance for the AaALDH3 genes quantified by quantitative PCR
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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
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
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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
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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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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baker, F.C.; MAuchamp, B.; Tsai, L.W.; Schooley, D.A.
Farnesol and farnesal dehydrogenase(s) in corpora allata of the tobacco hornworm moth, Manduca sexta
J. Lipid Res.
24
1586-1594
1983
Manduca sexta
brenda
Bede, J.C.; Teal, P.E.; Goodman, W.G.; Tobe, S.S.
Biosynthetic pathway of insect juvenile hormone III in cell suspension cultures of the sedge Cyperus iria
Plant Physiol.
127
584-593
2001
Cyperus iria
brenda
Rivera-Perez, C.; Nouzova, M.; Clifton, M.E.; Garcia, E.M.; Leblanc, E.; Noriega, F.G.
Aldehyde dehydrogenase 3 converts farnesal into farnesoic acid in the corpora allata of mosquitoes
Insect Biochem. Mol. Biol.
43
675-682
2013
Aedes aegypti, Aedes aegypti Rockefeller
brenda
Seman-Kamarulzaman, A.; Mohamed-Hussein, Z.; Ng, C.; Hassan, M.
Novel NAD+-farnesal dehydrogenase from Polygonum minus leaves. Purification and characterization of enzyme in juvenile hormone III biosynthetic pathway in plant
PLoS ONE
11
e0161707
2016
Persicaria minor
brenda
Rivera-Perez, C.; Nouzova, M.; Clifton, M.E.; Garcia, E.M.; LeBlanc, E.; Noriega, F.G.
Aldehyde dehydrogenase 3 converts farnesal into farnesoic acid in the corpora allata of mosquitoes
Insect Biochem. Mol. Biol.
43
675-682
2013
Aedes aegypti (Q16MV5), Aedes aegypti (Q16MV6), Aedes aegypti (Q16MV7), Aedes aegypti Rockefeller (Q16MV5), Aedes aegypti Rockefeller (Q16MV6), Aedes aegypti Rockefeller (Q16MV7)
brenda
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