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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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).
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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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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
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
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
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
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
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)