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
Comparison of expression of aldehyde dehydrogenase 3 and CYP1A1 in dominant and recessive aryl hydrocarbon hydroxylase-deficient mutant mouse hepatoma cells.
Promyelocytic leukemia protein induces arsenic trioxide resistance through regulation of aldehyde dehydrogenase 3 family member A1 in hepatocellular carcinoma.
Molecular Portrait of Metastasis-Competent Circulating Tumor Cells in Colon Cancer Reveals the Crucial Role of Genes Regulating Energy Metabolism and DNA Repair.
Promyelocytic leukemia protein induces arsenic trioxide resistance through regulation of aldehyde dehydrogenase 3 family member A1 in hepatocellular carcinoma.
Synergetic Bitherapy in Mice with Xenografts of Human Prostate Cancer Using a Methional Mimic (METLICO) and an Aldehyde Dehydrogenase 3 Inhibitor (MATE): Systemic Intraperitoneal (IP) and Targeted Intra-Tumoral (IT) Administration.
Synergetic Bitherapy in Mice with Xenografts of Human Prostate Cancer Using a Methional Mimic (METLICO) and an Aldehyde Dehydrogenase 3 Inhibitor (MATE): Systemic Intraperitoneal (IP) and Targeted Intra-Tumoral (IT) Administration.
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, determination of transcript abundance for the AaALDH3 genes 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, determination of transcript abundance for the AaALDH3 genes quantified by quantitative PCR
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, 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, 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, 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
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
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
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
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
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
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
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
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