Adaptive relationships of epoxide hydrolase in herbivorous arthropods

Christopher Albert Mullin

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Epoxide hydrolase catalyzes a simple hydrolysis of reactive cyclic ethers that may otherwise alkylate and impair critical proteins and nucleic acids required for life. Although much less studied than the cytochrome P-450 monooxygenases that produce epoxides, differences in subcellular, tissue, pH, substrate, and inhibitor specificities argue for at least three forms of insect epoxide hydrolase. Increasing numbers of epoxides are being identified as plant allelochemicals, antifeedants, and essential hormones or precursors for herbivorous arthropods, and in many cases an associated alkene to diol pathway of metabolism is found. A role for epoxide hydrolase in arthropod-plant interactions is strongly supported by species comparisons and by age-activity and induction studies. Two major limitations for study in biochemical ecology of epoxide hydrolase are the lack of an effective in vivo inhibitor and a range of commercially available radiolabeled substrates for the enzymes.

Original languageEnglish (US)
Pages (from-to)1867-1888
Number of pages22
JournalJournal of Chemical Ecology
Volume14
Issue number10
DOIs
StatePublished - Oct 1 1988

Fingerprint

epoxide hydrolase
Epoxide Hydrolases
Arthropods
arthropod
arthropods
inhibitor
antifeedant
substrate
allelochemical
alkene
Epoxy Compounds
nucleic acid
epoxides
ether
hormone
cytochrome
hydrolysis
Cyclic Ethers
metabolism
insect

All Science Journal Classification (ASJC) codes

  • Ecology, Evolution, Behavior and Systematics
  • Biochemistry

Cite this

Mullin, Christopher Albert. / Adaptive relationships of epoxide hydrolase in herbivorous arthropods. In: Journal of Chemical Ecology. 1988 ; Vol. 14, No. 10. pp. 1867-1888.
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Adaptive relationships of epoxide hydrolase in herbivorous arthropods. / Mullin, Christopher Albert.

In: Journal of Chemical Ecology, Vol. 14, No. 10, 01.10.1988, p. 1867-1888.

Research output: Contribution to journalArticle

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