Epoxidases Involved in the Biosynthesis of Type II Sex Pheromones
Epoxidases Involved in the Biosynthesis of Type II Sex Pheromones
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DOI:
10.1007/978-981-15-3082-1_8
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发表时间:
2020
期刊:
影响因子:
--
通讯作者:
T. Fujii;Y. Rong;Y. Ishikawa
中科院分区:
文献类型:
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作者:
T. Fujii;Y. Rong;Y. Ishikawa
In moth species that utilize alkenyl (type II) sex pheromones, selective epoxidation of double bonds in the alkene pheromone components confers further diversity on their chemical structures. Two arctiids, the fall webwormHyphantria cuneaand the mulberry tiger mothLemyra imparilis, use the same epoxyalkene, Z3,Z6,epo9-21:H, as the main pheromone component. In these species, we recently identified cytochrome P450s (CYPs) belonging to the CYP341 family as enzymes involved in the specific epoxidation of a Z9 double bond of the pheromone precursor Z3,Z6,Z9-21:H. Furthermore, a cytochrome P450 belonging to a different family, CYP340, was identified as an enzyme responsible for the specific epoxidation of a Z3 double bond of the pheromone precursor Z3,Z6,Z9-19:H in the Japanese giant looperAscotis selenaria, which uses epo3,Z6,Z9-19:H as the main pheromone component. These findings suggest that epoxidases (CYPs) with different regio-specificities evolved independently.