Aedes aegypti juvenile hormone acid methyl transferase, the ultimate enzyme in the biosynthetic pathway of juvenile hormone III, exhibits substrate control

Ekert, Evelien Van; Heylen, Kristof; Rougé, Pierre; Powell, Charles A.; Shatters, Robert G.; Smagghe, Guy; Borovsky, Dov

doi:10.1016/j.jinsphys.2014.03.001

Cited by 24 publications

(63 citation statements)

References 39 publications

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“…The core fold of SAM‐MTs is composed of alternating α ‐helices and β ‐strands . Comparisons with previous studies revealed that the typical SAM‐MT fold was present in the secondary structure of Ld JHAMT, which incorporated the alternation of nine α ‐helices and six β ‐strands (Fig. ).…”

Section: Resultsmentioning

confidence: 73%

“…JHAMT belongs to the SAM‐MT superfamily and utilises S ‐adenosylmethionine (SAM) to methylate its substrate (JH III or JHA III). A. aegypti JHAMT ( Aa JHAMT) methylates JHA III 5 times more rapidly than farnesoic acid (FA) and shows significant differences in lower methyl transferase (MT) activities towards the cis / trans / trans , cis / trans / cis and the trans / cis / cis isomers of JHA I, indicating that substrate chirality is important for proper alignment at the catalytic cavity and for efficient methyl transfer by SAM . Aa JHAMT has a highly conserved SAM binding motif (motif I) hh(D/E) hGxGxG, where h represents a hydrophobic residue .…”

Section: Resultsmentioning

confidence: 99%

“…Then, farnesol is oxidised to farnesal and farnesoic acid (FA) by two successive reactions catalysed by farnesol oxidase and farnesal dehydrogenase respectively. Finally, FA is converted to active JH III by two catalytic actions, an epoxidation (C10, 11) and a methyl transfer, under the catalysation of an epoxidase CYP15A1 and a JH acid methyltransferase (JHAMT) respectively …”

Section: Introductionmentioning

confidence: 99%

“…JHAMT orthologues have been characterised in coleopteran Tribolium castaneum , dipteran Aedes aegypti and Drosophila melanogaster , lepidopteran Bombyx mori and Samia cynthia ricini , hymenopteran Apis mellifera and orthopteran Schistocerca gregaria . In A. aegypti , application of a JHA, methoprene, impaired pupation .…”

Section: Introductionmentioning

confidence: 99%

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Knockdown of juvenile hormone acid methyl transferase severely affects the performance of Leptinotarsa decemlineata (Say) larvae and adults

Zhou

et al. 2015

Pest Management Science

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Section: Resultsmentioning

confidence: 73%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Knockdown of juvenile hormone acid methyl transferase severely affects the performance of Leptinotarsa decemlineata (Say) larvae and adults

Zhou

et al. 2015

Pest Management Science

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“…JHAMT has been mostly described in insects with the catalytic activity in the methylation of FA/JHA to MF/JH III (Li et al, 2013;Marchal et al, 2011;Mayoral et al, 2009;Shinoda and Itoyama, 2003;Van Ekert et al, 2014). However, in crustaceans, JHAMT has only been reported in the water flea D. pulex (Hui et al, 2010), D. magna and the shrimp N. denticulata (Sin et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

The potential role of juvenile hormone acid methyltransferase in methyl farnesoate (MF) biosynthesis in the swimming crab, Portunus trituberculatus

Xie

Tian

Liu

et al. 2016

Animal Reproduction Science

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Juvenile hormone (JH) and methyl farnesoate (MF) play essential roles in the development and reproduction of insects and crustaceans respectively. Juvenile hormone acid methyltransferase (JHAMT) catalyzes the methyl esterification in insect JH biosynthesis, while the corresponding step in crustacean MF biosynthesis was long thought to be catalyzed by farnesoic acid O-methyltransferase (FAMeT). However, the new discovery of JHAMT orthologs in crustaceans indicates that JHAMT may also play essential role in the MF biosynthesis in crustaceans. Here we cloned and characterized the full-length cDNA encoding JHAMT in the swimming crab Portunus trituberculatus (PtJHAMT). Sequence and structure analysis of PtJHAMT revealed that it was composed of a 6-stranded β sheet with 9 α helices, and contained a signature Sadenosyl-L-methionine (SAM) binding motif, which is the hallmark in all SAM dependent methyltransferases (SAM-MTs). Several active sites that are critical for the interaction of SAM and JH/FA substrate were also conserved in PtJHAMT. The gene expression of PtJHAMT was highly specific to the mandibular organ, which is the sole site of MF synthesis. PtJHAMT expression significantly increased in the late-vitellogenic stage and mature stage, which suggests a possible role of PtJHAMT in modulating ovarian development. The role of PtJHAMT and PtFAMeT in MF biosynthesis was further investigated by RNA interfering (RNAi). Injection of PtJHAMT and PtFAMeT dsRNA both led to a decrease in hemolymph MF titers. Injection of PtHMGR dsRNA caused the decrease in PtJHAMT expression, but had no effect on mRNA level of PtFAMeT. Together these results suggested that JHAMT and FAMeT are both involved in the MF biosynthesis in crustaceans, while the JHAMT is highly specific to FA substrate, and FAMeT may have more catalytic functions.

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Cloning and characterization of Aedes aegypti juvenile hormone epoxide hydrolases (JHEHs)

Borovsky

Ekert

Buytaert

et al. 2022

Arch Insect Biochem Physiol

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Juvenile hormone epoxide hydrolase (JHEH) plays an important role in the metabolism of juvenile hormone III (JH III) in insects. To study the role that JHEH plays in female Aedes aegypti JHEH 1, 2, and 3 complementary DNA (cDNAs) were cloned and sequenced. Northern blot analyses show that the three transcripts are expressed in the head thorax, the gut, the ovaries, and the fat body of females. Molecular modeling shows that the enzyme is a homodimer that binds JH III acid (JH IIIA) at the catalytic groove better than JH III. The cDNA of JHEH 1 and 2 are very similar indicating close relationship. Knocking down of jheh 1, 2, and 3 in adult female and larval Ae. aegypti using double‐stranded RNA (dsRNA) did not affect egg development or caused adult mortality. Larvae that were fed bacterial cells expressing dsRNA against jheh 1, 2, and 3 grew normally. Treating blood‐fed female Ae. aegypti with [12‐3H](10R) JH III and analyzing the metabolites by C18 reversed phase chromatography showed that JHEH preferred substrate is not JH III but JH IIIA. Genomic analysis of jheh 1, 2, and 3 indicate that jheh 1 and 2 are transcribed from a 1.53 kb DNA whereas jheh 3 is transcribed from a 10.9 kb DNA. All three genes are found on chromosome two at distinct locations. JHEH 2 was expressed in bacterial cells and purified by Ni affinity chromatography. Sequencing of the recombinant protein by MS/MS identified JHEH 2 as the expressed recombinant protein.

show abstract

Aedes aegypti juvenile hormone acid methyl transferase, the ultimate enzyme in the biosynthetic pathway of juvenile hormone III, exhibits substrate control

Cited by 24 publications

References 39 publications

Knockdown of juvenile hormone acid methyl transferase severely affects the performance of Leptinotarsa decemlineata (Say) larvae and adults

Knockdown of juvenile hormone acid methyl transferase severely affects the performance of Leptinotarsa decemlineata (Say) larvae and adults

The potential role of juvenile hormone acid methyltransferase in methyl farnesoate (MF) biosynthesis in the swimming crab, Portunus trituberculatus

Cloning and characterization of Aedes aegypti juvenile hormone epoxide hydrolases (JHEHs)

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