An Insect Juvenile Hormone-Specific Epoxide Hydrolase Is Related to Vertebrate Microsomal Epoxide Hydrolases

Wojtasek, Hubert; Prestwich, Glenn D.

doi:10.1006/bbrc.1996.0404

Cited by 64 publications

(50 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…37) So far, two definitive pathways have been described for the metabolic degradation of JH: hydration of the epoxide moiety by epoxide hydrolases and hydrolysis of the methyl ester moiety by soluble esterases. 35,[38][39][40] JH epoxide hydrolase (JHEH) was purified and characterized from the eggs of M. sexta, 41) and the cDNA has been cloned from lepidopteran species [42][43][44] and the cat flea Ctenocephalides felis. 45) Most of the research on JH metabolism has focused on JH esterases (JHE).…”

Section: Biosynthesis Transport and Metabolism Of Juvenile Hormonementioning

confidence: 99%

Insect juvenile hormone action as a potential target of pest management

Minakuchi

Riddiford

2006

J. Pestic. Sci.

View full text Add to dashboard Cite

Juvenile hormone (JH) is a sesquiterpenoid hormone that regulates growth and development in insects. Since JH is a hormone specific to insects and other arthropods, compounds disrupting JH action in insects are expected to be ideal insecticides with low toxicity to non-target organisms. Many natural or synthetic analogs with JH-like or anti-JH activity have been identified, and some potent JH mimics have been used as insecticides. Recent studies on the enzymes in JH biosynthetic and metabolic pathways should be helpful for the discovery of more potent analogs and for the establishment of new means of pest management using recombinant DNA technology. © Pesticide Science Society of Japan Keywords: juvenile hormone (JH), insect metamorphosis, insect growth regulators, biosynthesis and metabolism of JH. Review* To whom correspondence should be addressed. E-mail: chieka_minakuchi@yahoo.com © Pesticide Science Society of Japan doptera. 17,18) Higher Diptera such as D. melanogaster and the blowfly Calliphora vomitoria produce JH III bisepoxide. 19,20) A small amount of methyl farnesoate, a precursor of JH III, was found in cockroach embryos and larvae. [20][21][22] Methyl farnesoate has also been identified in crustaceans 23) and is thought to have a JH-like action in female reproduction. 24)12Ј-OH JH III identified from the corpora allata of the African locust Locusta migratoria migratorioides was reported to exhibit JH activity when a high dose of this compound was topically applied to Tenebrio pupae. 25,26) Biosynthesis, Transport and Metabolism of Juvenile HormoneIn insects, JH is synthesized in the corpora allata via the mevalonate pathway (Fig. 2).27) The mevalonate pathway also exists in mammals and plants, and the early steps from acetylCoA to farnesyl diphosphate are conserved among these organisms. Importantly, insects and other arthropods do not synthesize cholesterol de novo but have to acquire it from dietary sources because they lack the genes encoding squalene synthase and other subsequent enzymes of the sterol branch. 28,29) Another peculiarity of the mevalonate pathway in insects is the capacity to synthesize JH via the isoprenoid branch.The genes encoding the enzymes in the mevalonate pathway from acetyl-CoA to farnesyl diphosphate have been identified in the genome of D. melanogaster and the malaria mosquito Anopheles gambiae, and in an EST library of the pine engraver Ips pini.27) However, it has been difficult to identify the genes encoding enzymes from farnesyl diphosphate to JH

show abstract

Section: Biosynthesis Transport and Metabolism Of Juvenile Hormonementioning

confidence: 99%

Insect juvenile hormone action as a potential target of pest management

Minakuchi

Riddiford

2006

J. Pestic. Sci.

View full text Add to dashboard Cite

show abstract

“…Most research has focused on mammalian epoxide hydrolases since these enzymes are of toxicological relevance. The epoxide hydrolase genes that have been cloned so far are of mammalian, insect, and plant origin (1)(2)(3)(4)(5)(6)(7)(8)(9), and they can be distinguished into a class of microsomal enzymes and a class of soluble enzymes based on cellular localization and biochemical properties like substrate specificity. The mammalian epoxide hydrolases are believed to belong to the ␣/␤-hydrolase fold family (10 -12) since they show a low but significant sequence similarity with haloalkane dehalogenase from Xanthobacter autotrophicus GJ10 (13) of which the three-dimensional structure has been solved by x-ray crystallography (14).…”

mentioning

confidence: 99%

“…strain B (42); sEHs, soluble epoxide hydrolase from potato (7); sEHh, soluble epoxide hydrolase from human (1); BpA2, bromoperoxidase A2 from S. aereofaciens (44); DhlA, haloalkane dehalogenase from X. autotrophicus GJ10 (13); and mEHh, microsomal epoxide hydrolase from human (4). The other epoxide hydrolase sequences were omitted from the alignment due to high sequence similarity (over 80%) to the depicted epoxide hydrolases (2,3,5,6,8,9).…”

mentioning

confidence: 99%

Primary Structure and Catalytic Mechanism of the Epoxide Hydrolase from Agrobacterium radiobacterAD1

Rink

Fennema

Smids

et al. 1997

Journal of Biological Chemistry

161

169

View full text Add to dashboard Cite

The epoxide hydrolase gene from Agrobacterium radiobacter AD1, a bacterium that is able to grow on epichlorohydrin as the sole carbon source, was cloned by means of the polymerase chain reaction with two degenerate primers based on the N-terminal and C-terminal sequences of the enzyme. The epoxide hydrolase gene coded for a protein of 294 amino acids with a molecular mass of 34 kDa. An identical epoxide hydrolase gene was cloned from chromosomal DNA of the closely related strain A. radiobacter CFZ11. The recombinant epoxide hydrolase was expressed up to 40% of the total cellular protein content in Escherichia coli BL21(DE3) and the purified enzyme had a k cat of 21 s ؊1 with epichlorohydrin. Amino acid sequence similarity of the epoxide hydrolase with eukaryotic epoxide hydrolases, haloalkane dehalogenase from Xanthobacter autotrophicus GJ10, and bromoperoxidase A2 from Streptomyces aureofaciens indicated that it belonged to the ␣/␤-hydrolase fold family. This conclusion was supported by secondary structure predictions and analysis of the secondary structure with circular dichroism spectroscopy. The catalytic triad residues of epoxide hydrolase are proposed to be Asp 107 , His 275, and Asp 246 . Replacement of these residues to Ala/Glu, Arg/Gln, and Ala, respectively, resulted in a dramatic loss of activity for epichlorohydrin. The reaction mechanism of epoxide hydrolase proceeds via a covalently bound ester intermediate, as was shown by single turnover experiments with the His 275 3 Arg mutant of epoxide hydrolase in which the ester intermediate could be trapped.

show abstract

“…Most of these enzymes have important functions for the respective organisms being involved in the detoxification of xenobiotics, inflammation, and blood pressure regulation in mammals or the cutin biosynthesis in plants (25,26). In insects, EHs have been shown to degrade juvenile hormones (27,28) and to deactivate epoxide containing sex pheromones in moth antennae (29). In the context of pheromone biosynthesis, however, these enzymes have not, to our knowledge, been studied.…”

mentioning

confidence: 99%

An epoxide hydrolase involved in the biosynthesis of an insect sex attractant and its use to localize the production site

Abdel-latief

Garbe

Koch

et al. 2008

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

View full text Add to dashboard Cite

Epoxide hydrolases (EHs) are enzymes occurring in virtually any living organism. They catalyze the hydrolysis of epoxide containing lipids and are involved in crucial mechanisms, such as the detoxification of xenobiotics or the regulation of inflammation and blood pressure. Here, we describe a function of a putative EH gene in the biosynthesis of a sex attractant in the jewel wasp Nasonia vitripennis and use this gene to localize the site of pheromone production. Males of this parasitic wasp release a mixture of (4R,5R)-(Athreo-) and (4R,5S)-(Aerythro-)5-hydroxy-4-decanolide (HDL) to attract virgin females. Using a stable isotope labeled precursor, we demonstrated that vernolic acid (Aerythro-12,13-epoxy-octadec-9Z-enoic acid) is converted by N. vitripennis males to threo-HDL. This suggested the involvement of an EH in hydrolyzing the fatty acid epoxide under inversion of the stereochemistry into the respective diol, which might be further processed by chain shortening and lactonization to HDL. We cloned a putative N. vitripennis EH gene (Nasvi-EH1) encoding 470 amino acids and localized its transcripts in the male rectal papillae by in situ RT-PCR. Chemical analyses and histological studies confirmed that males synthesize the sex attractant in the rectal vesicle and release it via the anal orifice. Involvement of Nasvi-EH1 in HDL biosynthesis was established by RNAi-mediated gene silencing. Injection of Nasvi-EH1 dsRNA into male abdomens inhibited pheromone biosynthesis by 55% and suppressed the targeted gene transcripts in the rectal vesicle by 95%.Nasonia vitripennis ͉ pheromone biosynthesis ͉ pheromone gland

show abstract

An Insect Juvenile Hormone-Specific Epoxide Hydrolase Is Related to Vertebrate Microsomal Epoxide Hydrolases

Cited by 64 publications

References 0 publications

Insect juvenile hormone action as a potential target of pest management

Insect juvenile hormone action as a potential target of pest management

Primary Structure and Catalytic Mechanism of the Epoxide Hydrolase from Agrobacterium radiobacterAD1

An epoxide hydrolase involved in the biosynthesis of an insect sex attractant and its use to localize the production site

Contact Info

Product

Resources

About