Characterization of Hovi-Meh1, a microsomal epoxide hydrolase from the glassy-winged sharpshooter homalodisca vitripennis

Shizuo G. Kamita, Grant H. Oshita, Peng Wang, Christophe Morisseau, Bruce D. Hammock, Raja Sekhar Nandety, Bryce W. Falk

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Epoxide hydrolase (EH) is an enzyme in the α/β-hydrolase fold superfamily that uses a water molecule to transform an epoxide to its corresponding diol. In insects, EHs metabolize among other things critical developmental hormones called juvenile hormones (JHs). EHs also play roles in the detoxification of toxic compounds that are found in the insect's diet or environment. In this study, a full-length cDNA encoding an epoxide hydrolase, Hovi-mEH1, was obtained from the xylem-feeding insect Homalodisca vitripennis. H. vitripennis, commonly known as the glassy-winged sharpshooter, is an economically important vector of plant pathogenic bacteria such as Xylella fastidiosa. Hovi-mEH1 hydrolyzed the general EH substrates cis-stilbene oxide and trans-diphenylpropene oxide with specific activities of 47.5 ± 6.2 and 1.3 ± 0.5 nmol of diol formed min-1 mg-1, respectively. Hovi-mEH1 metabolized JH III with a Vmax of 29.3 ± 1.6 nmol min-1 mg-1, kcat of 0.03 s-1, and KM of 13.8 ± 2.0 μM. These Vmax and kcat values are similar to those of known JH metabolizing EHs from lepidopteran and coleopteran insects. Hovi-mEH1 showed 99.1% identity to one of three predicted EH-encoding sequences that were identified in the transcriptome of H. vitripennis. Of these three sequences only Hovi-mEH1 clustered with known JH metabolizing EHs. On the basis of biochemical, phylogenetic, and transcriptome analyses, we hypothesize that Hovi-mEH1 is a biologically relevantJH-metabolizing enzyme in H. vitripennis.

Original languageEnglish (US)
Pages (from-to)171-179
Number of pages9
JournalArchives of Insect Biochemistry and Physiology
Volume83
Issue number4
DOIs
StatePublished - Aug 2013

Fingerprint

epoxide hydrolase
Homalodisca vitripennis
Epoxide Hydrolases
Juvenile Hormones
Insects
juvenile hormones
glycols
insects
Xylella
transcriptome
oxides
Xylem
Detoxification
Poisons
Epoxy Compounds
Hormones
Gene Expression Profiling
Hydrolases
Enzymes
Xylella fastidiosa

Keywords

  • Epoxide hydrolase
  • GWSS
  • Homalodisca vitripennis
  • Juvenile hormone

ASJC Scopus subject areas

  • Insect Science
  • Physiology
  • Biochemistry

Cite this

Characterization of Hovi-Meh1, a microsomal epoxide hydrolase from the glassy-winged sharpshooter homalodisca vitripennis. / Kamita, Shizuo G.; Oshita, Grant H.; Wang, Peng; Morisseau, Christophe; Hammock, Bruce D.; Nandety, Raja Sekhar; Falk, Bryce W.

In: Archives of Insect Biochemistry and Physiology, Vol. 83, No. 4, 08.2013, p. 171-179.

Research output: Contribution to journalArticle

Kamita, Shizuo G. ; Oshita, Grant H. ; Wang, Peng ; Morisseau, Christophe ; Hammock, Bruce D. ; Nandety, Raja Sekhar ; Falk, Bryce W. / Characterization of Hovi-Meh1, a microsomal epoxide hydrolase from the glassy-winged sharpshooter homalodisca vitripennis. In: Archives of Insect Biochemistry and Physiology. 2013 ; Vol. 83, No. 4. pp. 171-179.
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abstract = "Epoxide hydrolase (EH) is an enzyme in the α/β-hydrolase fold superfamily that uses a water molecule to transform an epoxide to its corresponding diol. In insects, EHs metabolize among other things critical developmental hormones called juvenile hormones (JHs). EHs also play roles in the detoxification of toxic compounds that are found in the insect's diet or environment. In this study, a full-length cDNA encoding an epoxide hydrolase, Hovi-mEH1, was obtained from the xylem-feeding insect Homalodisca vitripennis. H. vitripennis, commonly known as the glassy-winged sharpshooter, is an economically important vector of plant pathogenic bacteria such as Xylella fastidiosa. Hovi-mEH1 hydrolyzed the general EH substrates cis-stilbene oxide and trans-diphenylpropene oxide with specific activities of 47.5 ± 6.2 and 1.3 ± 0.5 nmol of diol formed min-1 mg-1, respectively. Hovi-mEH1 metabolized JH III with a Vmax of 29.3 ± 1.6 nmol min-1 mg-1, kcat of 0.03 s-1, and KM of 13.8 ± 2.0 μM. These Vmax and kcat values are similar to those of known JH metabolizing EHs from lepidopteran and coleopteran insects. Hovi-mEH1 showed 99.1{\%} identity to one of three predicted EH-encoding sequences that were identified in the transcriptome of H. vitripennis. Of these three sequences only Hovi-mEH1 clustered with known JH metabolizing EHs. On the basis of biochemical, phylogenetic, and transcriptome analyses, we hypothesize that Hovi-mEH1 is a biologically relevantJH-metabolizing enzyme in H. vitripennis.",
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AU - Wang, Peng

AU - Morisseau, Christophe

AU - Hammock, Bruce D.

AU - Nandety, Raja Sekhar

AU - Falk, Bryce W.

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