Farnesol metabolism in Drosophila melanogaster: Ontogeny and tissue distribution of octanol dehydrogenase and aldehyde oxidase

Madhavan, Kornath; Conscience-Egli, M; Sieber, Fritz; Ursprung, Heinrich W.

doi:10.1016/0022-1910(73)90236-9

Cited by 29 publications

(15 citation statements)

References 11 publications

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“…Moreover, the present results identify octanol dehydrogenase, which has been discussed previously (16)(17)(18)(19)(20) but with somewhat contradictory estimates regarding molecular weight and quaternary structure, as being identical to the class III medium-chain alcohol dehydrogenase. Thus, the octanol dehydrogenase is involved also in glutathionedependent elimination of formaldehyde.…”

Section: Resultsmentioning

confidence: 62%

“…The other is active with octanol and formaldehyde/glutathione in a manner typical of mammalian medium-chain class III alcohol dehydrogenase. This suggests that the zinc-containing class III enzyme is present in Drosophila and that this glutathionedependent formaldehyde dehydrogenase may represent the little-studied Drosophila octanol dehydrogenase previously reported (16)(17)(18)(19)(20) but not characterized structurally.…”

Section: Resultsmentioning

confidence: 88%

“…We now show that the family is indeed present also in insects and that its major representative is the typical class III type. In fact, the enzyme turns out to be identical to Drosophila octanol dehydrogenase, long known (16)(17)(18)(19)(20) but little studied. We have characterized the enzyme from Drosophila melanogaster enzymatically and structurally to prove its consistency with other class III forms.…”

Section: Introductionmentioning

confidence: 99%

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Fundamental molecular differences between alcohol dehydrogenase classes.

Danielsson

Atrian

Luque

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

135

128

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Two types of alcohol dehydrogenase in separate protein families are the "medium-chain" zinc enzymes (including the classical liver and yeast forms) and the "shortchain" enzymes (including the insect form). Although the medium-chain family has been characterized in prokaryotes and many eukaryotes (fungi, plants, cephalopods, and verte-brates), insects have seemed to possess only the short-chain enzyme. We have now also characterized a medium-chain alcohol dehydrogenase in Drosophila. The developmental stages of the fly, compatible with the constitutive nature of the vertebrate enzyme. Taken together, the results bridge a previously apparent gap in the distribution of medium-chain alcohol dehydrogenases and establish a strictly conserved class m enzyme, consistent with an important role for this enzyme in cellular metabolism.The "classical" alcohol dehydrogenase is part of a widespread system of zinc-containing enzymes (1). In mammalian tissues, at least six classes of this enzyme occur. They differ considerably and represent stages between separate enzymes and ordinary isozymes. Class I is the well-known liver enzyme with ethanol dehydrogenase activity (2), class III is identical with glutathione-dependent formaldehyde dehydrogenase (3), class IV is a form preferentially expressed in stomach (4, 5), while classes II, V, and VI, although little studied, are known also to exhibit distinct properties (6, 7, 44). The class origins have been traced to gene duplications early in vertebrate evolution [the I/III duplication (8)] or during that evolution [the IV/I duplication (5)], with emerging activities toward ethanol (9); class III corresponds to an ancestral form. These properties and the different evolutionary patterns, with class III being "constant" and class I "variable" (10), result in a consistent picture of the enzyme system and place the classes of medium-chain alcohol dehydrogenases as separate enzymes in the cellular metabolism.Similarly, another protein family, short-chain dehydrogenases, has also evolved into a family comprising many different enzyme activities, including an alcohol dehydrogenase (11). This form operates by means of a completely different catalytic mechanism and is related to mammalian prostaglandin dehydrogenases/carbonyl reductase (12). Thus far, this alcohol dehydrogenase has been found in insects, the Drosophila enzyme being recognized early to differ from the zinc-containing alcohol dehydrogenases (13,14). Its properties in various Drosophila species are well established (15).These two alcohol dehydrogenase types demonstrate that ethanol dehydrogenase activity has evolved in different manners, with many organisms now employing a medium-chain enzyme, while others depend on a short-chain enzyme. The medium-chain family has not been identified in insects, although it is of ancient origin and has been characterized in other eukaryotes and in prokaryotes. We now show that the family is indeed present also in insects and that its major representative is the typical class III t...

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Section: Resultsmentioning

confidence: 62%

Section: Resultsmentioning

confidence: 88%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Fundamental molecular differences between alcohol dehydrogenase classes.

Danielsson

Atrian

Luque

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

135

128

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“…Visualization of farnesol dehydrogenase activity in PAGE and whole mount CA preparations were performed as described by Madhavan et al (42). CA were isolated as described in ref.…”

Section: Methodsmentioning

confidence: 99%

NADP ⁺ -dependent farnesol dehydrogenase, a corpora allata enzyme involved in juvenile hormone synthesis

Mayoral

Nouzová

Navare

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

107

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The synthesis of juvenile hormone (JH) is an attractive target for control of insect pests and vectors of disease, but the minute size of the corpora allata (CA), the glands that synthesize JH, has made it difficult to identify important biosynthetic enzymes by classical biochemical approaches. Here, we report identification and characterization of an insect farnesol dehydrogenase (AaSDR-1) that oxidizes farnesol into farnesal, a precursor of JH, in the CA. AaSDR-1 was isolated as an EST in a library of the corpora allata-corpora cardiaca of the mosquito Aedes aegypti. The 245-amino acid protein presents the typical short-chain dehydrogenase (SDR) Rossmann-fold motif for nucleotide binding. This feature, together with other conserved sequence motifs, place AaSDR-1 into the ''classical'' NADP ؉ -dependent cP2 SDR subfamily. The gene is part of a group of highly conserved paralogs that cluster together in the mosquito genome; similar clusters of orthologs were found in other insect species. AaSDR-1 acts as a homodimer and efficiently oxidizes C 10 to C15 isoprenoid and aliphatic alcohols, showing the highest affinity for the conversion of farnesol into farnesal. Farnesol dehydrogenase activity was not detected in the CA of newly emerged mosquitoes but significant activity was detected 24 h later. Real time PCR experiments revealed that AaSDR-1 mRNA levels were very low in the inactive CA of the newly emerged female, but increased >30-fold 24 h later during the peak of JH synthesis. These results suggest that oxidation of farnesol might be a rate-limiting step in JH III synthesis in adult mosquitoes.mosquito ͉ Aedes ͉ farnesal ͉ insect

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“…However, this oxidation may instead be catalyzed by a specific alcohol oxidase (Sperry and Sen, 2001). Strong staining for farnesol dehydrogenase activity and farnesal oxidase activity has been observed in the CA portion of larval ring glands of a Drosophila mutant lacking alcohol dehydrogenase (Madhavan et al, 1973). In the Aedes EST collection, we found an ortholog of the B. mori JH acid methyl transferase (Shinoda and Itoyama, 2003), and, interestingly, for an homolog of the sequence described as a farnesoic acid O-methyltransferase in Crustacea (Gunawardene et al, 2002) as well.…”

mentioning

confidence: 99%

Comparative genomics of insect juvenile hormone biosynthesis☆

Noriega

Ribeiro

Koener

et al. 2006

Insect Biochemistry and Molecular Biology

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The biosynthesis of insect juvenile hormone (JH) and its neuroendocrine control are attractive targets for chemical control of insect pests and vectors of disease. To facilitate the molecular study of JH biosynthesis, we analyzed ESTs from the glands producing JH, the corpora allata (CA) in the cockroach Diploptera punctata, an insect long used as a physiological model species and compared them with ESTs from the CA of the mosquitoes Aedes aegypti and Anopheles albimanus. The predicted genes were analyzed according to their probable functions with the Gene Ontology classification, and compared to Drosophila and Anopheles gambiae genes. A large number of reciprocal matches in the cDNA libraries of cockroach and mosquito CA were found. These matches defined known and suspected enzymes of the JH biosynthetic pathway, but also several proteins associated with signal transduction that might play a role in the modulation of JH synthesis by neuropeptides. The identification in both cockroach and mosquito CA of homologs of the small ligand binding proteins from insects, Takeout/JH binding protein and retinol-binding protein highlights a hitherto unsuspected complexity of metabolite trafficking, perhaps JH precursor trafficking, in these endocrine glands. Furthermore, many reciprocal matches for genes of unknown function may provide a fertile ground for an in-depth study of allatal-specific cell physiology.

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Farnesol metabolism in Drosophila melanogaster: Ontogeny and tissue distribution of octanol dehydrogenase and aldehyde oxidase

Cited by 29 publications

References 11 publications

Fundamental molecular differences between alcohol dehydrogenase classes.

Fundamental molecular differences between alcohol dehydrogenase classes.

NADP ⁺ -dependent farnesol dehydrogenase, a corpora allata enzyme involved in juvenile hormone synthesis

Comparative genomics of insect juvenile hormone biosynthesis☆

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Farnesol metabolism in Drosophila melanogaster: Ontogeny and tissue distribution of octanol dehydrogenase and aldehyde oxidase

Cited by 29 publications

References 11 publications

Fundamental molecular differences between alcohol dehydrogenase classes.

Fundamental molecular differences between alcohol dehydrogenase classes.

NADP + -dependent farnesol dehydrogenase, a corpora allata enzyme involved in juvenile hormone synthesis

Comparative genomics of insect juvenile hormone biosynthesis☆

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Product

Resources

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NADP ⁺ -dependent farnesol dehydrogenase, a corpora allata enzyme involved in juvenile hormone synthesis