Characterization and Activity Change of Farnesol Dehydrogenase in Black Rot Fungus-infected Sweet Potato

Inoue, Hiromasa; Tsuji, Hiroko; Uritani, Ikuzô

doi:10.1080/00021369.1984.10866210

Cited by 7 publications

(33 citation statements)

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“…Similar farnesol dehydrogenases that oxidize farnesol, as well as C 10 to C 15 isoprenoid and aliphatic compounds have been described in sweet potato (17) and human liver (18).…”

Section: Aasdr-1 Efficiently Oxidizes Farnesol To Farnesalmentioning

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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“…Similar farnesol dehydrogenases that oxidize farnesol, as well as C 10 to C 15 isoprenoid and aliphatic compounds have been described in sweet potato (17) and human liver (18).…”

Section: Aasdr-1 Efficiently Oxidizes Farnesol To Farnesalmentioning

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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“…Because the substrate profile of the FLDH-encoded farnesol dehydrogenase does not match the substrate profile observed in Arabidopsis membranes (i.e. geranylgeraniol is the preferred substrate when Arabidopsis membranes are used, but farnesol is the preferred substrate of the FLDHencoded enzyme), it is likely that the activity detected in Arabidopsis membranes represents multiple dehydrogenases, including a geranylgeraniol dehydrogenase and possibly an NADP + -dependent farnesol dehydrogenase (Inoue et al, 1984;Mayoral et al, 2009). In addition, our data suggest that the FLDHencoded farnesol dehydrogenase catalyzes farnesol oxidation rather than farnesal reduction.…”

Section: Discussionmentioning

confidence: 99%

“…To date, farnesol dehydrogenase activity has only been described in insect corpora allata glands and black rot fungus-infected potato (Baker et al, 1983;Inoue et al, 1984;Sperry and Sen, 2001;Mayoral et al, 2009). Moreover, the only gene known to encode a protein with farnesol dehydrogenase activity belongs to the short-chain dehydrogenase gene family from mosquito (AaSDR-1; Mayoral et al, 2009).…”

Section: Identification Of An Arabidopsis Farnesol Dehydrogenase Genementioning

confidence: 99%

“…1; Thai et al, 1999;Crowell et al, 2007). To date, the only reports of such an oxidoreductase are from the corpora allata glands of insects, where it participates in juvenile hormone synthesis, and black rot fungus-infected sweet potato (Ipomoea batatas; Baker et al, 1983;Inoue et al, 1984;Sperry and Sen, 2001;Mayoral et al, 2009). Insect farnesol dehydrogenase is an NADP + -dependent oxidoreductase that is encoded by a subfamily of shortchain dehydrogenase/reductase (SDR) genes (Mayoral et al, 2009).…”

mentioning

confidence: 99%

“…Insect farnesol dehydrogenase is an NADP + -dependent oxidoreductase that is encoded by a subfamily of shortchain dehydrogenase/reductase (SDR) genes (Mayoral et al, 2009). Farnesol dehydrogenase from sweet potato is a 90-kD, NADP + -dependent homodimer with broad specificity for prenyl alcohol substrates and is induced by wounding and fungus infection of potato roots (Inoue et al, 1984).…”

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confidence: 99%

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Identification of a Novel Abscisic Acid-Regulated Farnesol Dehydrogenase from Arabidopsis

2010

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In Arabidopsis (Arabidopsis thaliana), farnesylcysteine is oxidized to farnesal and cysteine by a membrane-associated thioether oxidase called farnesylcysteine lyase. Farnesol and farnesyl phosphate kinases have also been reported in plant membranes. Together, these observations suggest the existence of enzymes that catalyze the interconversion of farnesal and farnesol. In this report, Arabidopsis membranes are shown to possess farnesol dehydrogenase activity. In addition, a gene on chromosome 4 of the Arabidopsis genome (At4g33360), called FLDH, is shown to encode an NAD + -dependent dehydrogenase that oxidizes farnesol more efficiently than other prenyl alcohol substrates. FLDH expression is repressed by abscisic acid (ABA) but is increased in mutants with T-DNA insertions in the FLDH 5# flanking region. These T-DNA insertion mutants, called fldh-1 and fldh-2, are associated with an ABA-insensitive phenotype, suggesting that FLDH is a negative regulator of ABA signaling.

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Isolation, purification and biochemical characterization of Conopomorpha cramerella farnesol dehydrogenase

Satyaveanthan

Awang

et al. 2022

Insect Molecular Biology

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In Southeast Asia, Conopomorpha cramerella (Snellen) which is commonly known as the cocoa pod borer (CPB) moth has been identified as the most detrimental pest of Theobroma cacao L. Apart from the various side effects on human health and non-target organisms, heavily relying on synthetic pyrethroid insecticides to control CPB infestations also increases the environmental contamination risks. Thus, developing biorational insecticides that minimally affect the non-target organism and environment by targeting the insect growth regulation process is needed to manage the pest population. In insects, juvenile hormones (JH) regulate critical biological events, especially metamorphosis, development and reproduction. Since the physiological roles of JH III vary among different organisms, the biochemical properties, especially substrate specificity and analogue inhibition, may also be different. Therefore, studies on the JH III biosynthetic pathway enzymes in both plants and insects are beneficial to discover more effective analogues.Bioinformatic analysis and biochemical characterization of a NADP + -dependent farnesol dehydrogenase, an intermediate enzyme of the JH III pathway, from C. cramerella (CcFolDH), were described in this study. In addition, the farnesol analogues that may act as a potent analogue inhibitor for CcFolDH ware determined using in vitro enzymatic study. The phylogenetic analysis indicated that CcFolDH shared a close phylogenetic relationship to the honeybee's short-chain dehydrogenase/reductase. The 27 kDa CcFolDH has an NADP(H) binding domain with a typical Rossmann fold and is likely a homotetrameric protein in the solution. The enzyme had a greater preference for substrate trans, trans-farnesol and coenzyme NADP + . In terms of analogue inhibitor inhibition, hexahydroxyfarnesyl acetone showed the highest inhibition (the lowest K i ) compared to other farnesol analogues. Thus, hexahydroxyfarnesyl acetone would serve as the most potent active ingredient for future biorational pesticide management for C. cramerella infestation. Based on the bioinformatic analyses and biochemical characterizations conducted in this research, we proposed that rCcFolDH differs slightly from other reported farnesol dehydrogenases in terms of molecular weight, substrate preference, coenzymes utilization and analogue inhibitors selection.

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Characterization and Activity Change of Farnesol Dehydrogenase in Black Rot Fungus-infected Sweet Potato

Cited by 7 publications

References 2 publications

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

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

Identification of a Novel Abscisic Acid-Regulated Farnesol Dehydrogenase from Arabidopsis

Isolation, purification and biochemical characterization of Conopomorpha cramerella farnesol dehydrogenase

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Characterization and Activity Change of Farnesol Dehydrogenase in Black Rot Fungus-infected Sweet Potato

Cited by 7 publications

References 2 publications

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

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

Identification of a Novel Abscisic Acid-Regulated Farnesol Dehydrogenase from Arabidopsis

Isolation, purification and biochemical characterization of Conopomorpha cramerella farnesol dehydrogenase

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

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