Laboratory of Applied Entomology, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo 113-8657, Japan.
Proc Natl Acad Sci U S A. 2011 Apr 26;108(17):7102-6. doi: 10.1073/pnas.1019519108. Epub 2011 Mar 28.
(E)-11- and (Z)-11-tetradecenyl acetate are the most common female sex pheromone components in Ostrinia moths. The Δ11-desaturase expressed in the pheromone gland (PG) of female moths is a key enzyme that introduces a double bond into pheromone molecules. A single Δ11-desaturase of Ostrinia nubilalis, OnubZ/E11, has been shown to produce an ∼7:3 mixture of (E)-11- and (Z)-11-tetradecenoate from the substrate tetradecanoate. In contrast, the sex pheromone of Ostrinia latipennis, a primitive species of Ostrinia, is (E)-11-tetradecenol. This pheromone is unique in that it is not acetylated, and includes no Z isomer. In the present study, through the cloning and functional analysis of a PG-specific Δ11-desaturase in O. latipennis, we showed that the absence of the Z isomer in the pheromone is attributable to the strict product specificity of the Δ11-desaturase in this species, LATPG1. Phylogenetic analysis revealed that LATPG1 was not closely related to OnubZ/E11. Rather, it was closely related to retroposon-linked cryptic Δ11-desaturases (ezi-Δ11) found in the genomes of O. nubilalis and Ostrinia furnacalis. Taken together, the results showed that an unusual Δ11-desaturase is functionally expressed in O. latipennis, although the genes encoding this enzyme appear to be cryptic in congeners.
(E)-11-和(Z)-11-十四碳烯基乙酸酯是夜蛾科昆虫雌性性信息素中最常见的成分。在雌性蛾的信息素腺（PG）中表达的Δ11-去饱和酶是一种将双键引入信息素分子的关键酶。已经表明，一种来自十四烷酸的单Δ11-去饱和酶 Ostrinia nubilalis 的 OnubZ/E11，产生(E)-11-和(Z)-11-十四碳烯酸的大约 7:3 混合物。相比之下，Ostrinia latipennis 的性信息素，一种原始的夜蛾种类，是(E)-11-十四碳烯醇。这种信息素是独特的，因为它没有乙酰化，也没有 Z 异构体。在本研究中，通过对 O. latipennis 的 PG 特异性 Δ11-去饱和酶的克隆和功能分析，我们表明信息素中没有 Z 异构体是由于该物种 LATPG1 的 Δ11-去饱和酶的严格产物特异性。系统发育分析表明，LATPG1 与 OnubZ/E11 没有密切关系。相反，它与在 O. nubilalis 和 Ostrinia furnacalis 基因组中发现的 retroposon 相关的隐式 Δ11-去饱和酶（ezi-Δ11）密切相关。总之，结果表明，一种不寻常的 Δ11-去饱和酶在 O. latipennis 中具有功能性表达，尽管编码这种酶的基因在同属种中似乎是隐式的。
