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Literature summary for 1.2.1.94 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)

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

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/ Products (Substrates)

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 Stability

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

Organism

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

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 and Products (Substrate)

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

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

pH Optimum

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

Cofactor

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

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