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Literature summary extracted from

  • 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 (2013), Insect Biochem. Mol. Biol., 43, 675-682 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.94 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
1.2.1.94 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
1.2.1.94 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

EC Number Protein Variants Comment Organism
1.2.1.94 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
1.2.1.94 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.94 (2E,6E)-farnesal + NAD+ + H2O Aedes aegypti
-
 (2E,6E)-farnesoic acid + NADH + 2 H+
-
 ?
1.2.1.94 (2E,6E)-farnesal + NAD+ + H2O Aedes aegypti Rockefeller
-
 (2E,6E)-farnesoic acid + NADH + 2 H+
-
 ?

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
1.2.1.94 hexane enzyme inactivation at about 40% v/v hexane Aedes aegypti

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.94 Aedes aegypti Q16MV5
-
-
1.2.1.94 Aedes aegypti Q16MV6
-
-
1.2.1.94 Aedes aegypti Q16MV7
-
-
1.2.1.94 Aedes aegypti Rockefeller Q16MV5
-
-
1.2.1.94 Aedes aegypti Rockefeller Q16MV6
-
-
1.2.1.94 Aedes aegypti Rockefeller Q16MV7
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.94 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
-
1.2.1.94 additional information the enzyme shows tissue and developmental-stage-specific splice variants Aedes aegypti
-
1.2.1.94 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
-
1.2.1.94 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 and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.94 (2E,6E)-farnesal + NAD+ + H2O
-
 Aedes aegypti (2E,6E)-farnesoic acid + NADH + 2 H+
-
 ?
1.2.1.94 (2E,6E)-farnesal + NAD+ + H2O
-
 Aedes aegypti Rockefeller (2E,6E)-farnesoic acid + NADH + 2 H+
-
 ?
1.2.1.94 decanal + NAD+ + H2O
-
 Aedes aegypti decanoic acid + NADH + 2 H+
-
 ?
1.2.1.94 decanal + NAD+ + H2O
-
 Aedes aegypti Rockefeller decanoic acid + NADH + 2 H+
-
 ?
1.2.1.94 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 ?
-
 ?
1.2.1.94 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 ?
-
 ?
1.2.1.94 octanal + NAD+ + H2O
-
 Aedes aegypti octanoic acid + NADH + 2 H+
-
 ?
1.2.1.94 octanal + NAD+ + H2O
-
 Aedes aegypti Rockefeller octanoic acid + NADH + 2 H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.94 AaALDH3
-
 Aedes aegypti
1.2.1.94 AaALDH3-1
-
 Aedes aegypti
1.2.1.94 AaALDH3-2
-
 Aedes aegypti
1.2.1.94 AaeL_AAEL012161
-
 Aedes aegypti
1.2.1.94 AaeL_AAEL012162
-
 Aedes aegypti
1.2.1.94 AaeL_AAEL012165
-
 Aedes aegypti
1.2.1.94 NAD+-dependent class 3 ALDH
-
 Aedes aegypti

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.94 37
-
 assay at Aedes aegypti

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.94 9.5
-
 assay at Aedes aegypti

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.94 additional information AaALDH3s oxidizes farnesal to FA in the presence of NAD+, and NADP+ cannot substitute for NAD+ Aedes aegypti
1.2.1.94 NAD+ dependent on Aedes aegypti

General Information

EC Number General Information Comment Organism
1.2.1.94 evolution the enzyme is a member of the NAD+-dependent class 3 ALDH family of the aldehyde dehydrogenase superfamily Aedes aegypti
1.2.1.94 malfunction reduction of AaALDH3 activity results in accumulation of farnesal and conversion back to farnesol that leaks outside the corpora allata Aedes aegypti
1.2.1.94 metabolism the enzyme is a biosynthetic enzyme of the juvenile hormone JH pathway Aedes aegypti
1.2.1.94 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