Cloned (Comment) | Organism |
---|---|
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 | Aedes aegypti |
gene AaALDH3-2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, the enzyme shows tissue and developmental-stage-specific splice variants | Aedes aegypti |
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 | Aedes aegypti |
Protein Variants | Comment | Organism |
---|---|---|
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 | Aedes aegypti |
additional information | 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 | Aedes aegypti |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2E,6E)-farnesal + NAD+ + H2O | Aedes aegypti | - |
(2E,6E)-farnesoic acid + NADH + 2 H+ | - |
? | |
(2E,6E)-farnesal + NAD+ + H2O | Aedes aegypti Rockefeller | - |
(2E,6E)-farnesoic acid + NADH + 2 H+ | - |
? |
Organic Solvent | Comment | Organism |
---|---|---|
hexane | enzyme inactivation at about 40% v/v hexane | Aedes aegypti |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aedes aegypti | Q16MV5 | - |
- |
Aedes aegypti | Q16MV6 | - |
- |
Aedes aegypti | Q16MV7 | - |
- |
Aedes aegypti Rockefeller | Q16MV5 | - |
- |
Aedes aegypti Rockefeller | Q16MV6 | - |
- |
Aedes aegypti Rockefeller | Q16MV7 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
corpora allata | 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 | Aedes aegypti | - |
additional information | the enzyme shows tissue and developmental-stage-specific splice variants | Aedes aegypti | - |
additional information | the enzyme shows tissue and developmental-stage-specific splice variants, determination of transcript abundance for the AaALDH3 genes quantified by quantitative PCR | Aedes aegypti | - |
additional information | 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 | Aedes aegypti | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2E,6E)-farnesal + NAD+ + H2O | - |
Aedes aegypti | (2E,6E)-farnesoic acid + NADH + 2 H+ | - |
? | |
(2E,6E)-farnesal + NAD+ + H2O | - |
Aedes aegypti Rockefeller | (2E,6E)-farnesoic acid + NADH + 2 H+ | - |
? | |
decanal + NAD+ + H2O | - |
Aedes aegypti | decanoic acid + NADH + 2 H+ | - |
? | |
decanal + NAD+ + H2O | - |
Aedes aegypti Rockefeller | decanoic acid + NADH + 2 H+ | - |
? | |
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 | Aedes aegypti | ? | - |
? | |
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 | Aedes aegypti Rockefeller | ? | - |
? | |
octanal + NAD+ + H2O | - |
Aedes aegypti | octanoic acid + NADH + 2 H+ | - |
? | |
octanal + NAD+ + H2O | - |
Aedes aegypti Rockefeller | octanoic acid + NADH + 2 H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AaALDH3 | - |
Aedes aegypti |
AaALDH3-1 | - |
Aedes aegypti |
AaALDH3-2 | - |
Aedes aegypti |
AaeL_AAEL012161 | - |
Aedes aegypti |
AaeL_AAEL012162 | - |
Aedes aegypti |
AaeL_AAEL012165 | - |
Aedes aegypti |
NAD+-dependent class 3 ALDH | - |
Aedes aegypti |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Aedes aegypti |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9.5 | - |
assay at | Aedes aegypti |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | AaALDH3s oxidizes farnesal to FA in the presence of NAD+, and NADP+ cannot substitute for NAD+ | Aedes aegypti | |
NAD+ | dependent on | Aedes aegypti |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme is a member of the NAD+-dependent class 3 ALDH family of the aldehyde dehydrogenase superfamily | Aedes aegypti |
malfunction | reduction of AaALDH3 activity results in accumulation of farnesal and conversion back to farnesol that leaks outside the corpora allata | Aedes aegypti |
metabolism | the enzyme is a biosynthetic enzyme of the juvenile hormone JH pathway | Aedes aegypti |
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 | Aedes aegypti |