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Function, diversity, and application of insect juvenile hormone epoxidases (CYP15)
Author(s) -
Daimon Takaaki,
Shinoda Tetsuro
Publication year - 2013
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.1058
Subject(s) - juvenile hormone , biology , metamorphosis , lineage (genetic) , biochemistry , gene , insect , cytochrome p450 , enzyme , genetics , hormone , botany , larva
Juvenile hormones ( JH s) represent a family of sesquiterpenoid hormones in insects, and they play a key role in regulating development, metamorphosis, and reproduction. The last two steps of the JH biosynthetic pathway, epoxidation and methyl esterification of farnesoic acid to JH , are insect specific, and thus have long been considered a promising target for biorational insecticides. Recently, the enzymes involved in the last two steps have been molecularly identified: JH acid methyltransferase catalyzes the esterification step and the cytochrome P 450 CYP 15 enzyme catalyzes the epoxidation step. In this review, we describe the recent progress on the characterization of JH biosynthetic enzymes, with special focus on the function and diversity of the CYP 15 family. CYP 15 genes have evolved lineage‐specific substrate specificity and regulatory mechanisms in insects, which appear to be associated with the lineage‐specific acquisition of unique JH structure and function. In addition, the lack of CYP 15 genes in crustacean ( D aphnia pulex ) and arachnid ( T etranychus urticae ) species, whose genomes have been fully sequenced, may imply that CYP 15 enzymes are an evolutionary innovation in insects to use the epoxide forms of methylated farnesoid molecules as their principal JH s. Molecular identification and characterization of CYP 15 genes from broad taxa of insects have paved the way to the design of target‐specific, biorational anti‐ JH agents.