An insect juvenile hormone-specific epoxide hydrolase is related to vertebrate microsomal epoxide hydrolases.
We describe the first cDNA sequence encoding a juvenile hormone-specific epoxide hydrolase from an insect. A full-length cDNA clone revealed a 462-amino-acid open reading frame encoding an amino acid sequence with 44% identity and 64% similarity to human microsomal epoxide hydrolase. All residues in the catalytic triad (residues Asp227-His428-Asp350 in the M. sexta protein) were present, as was the conserved Trp154 corresponding to the oxyanion hole. The surprising similarity of insect juvenile hormone epoxide hydrolase to vertebrate microsomal epoxide hydrolases, coupled with the ancient lineage of the epoxide hydrolases and haloalkane dehalogenases, suggests that this catabolic enzyme evolved from an original ubiquitous detoxication function to a more recent role in hormonal regulation.
Wojtasek
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Department of Chemistry and Biochemistry, University at Stony Brook, New York 11794-3400, USA.
Prestwich
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GD
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D017124:Conserved Sequence; D018076:DNA, Complementary / Q000737:chemistry*; D004851:Epoxide Hydrolases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D007605:Juvenile Hormones / Q000378:metabolism*; D051379:Mice; D008861:Microsomes / Q000201:enzymology; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D016133:Polymerase Chain Reaction; D011817:Rabbits; D051381:Rats; D017385:Sequence Homology
D018076:DNA, Complementary; D007605:Juvenile Hormones; D004851:Epoxide Hydrolases