Aldehyde reductase activity in the antennae of Helicoverpa armigera
Aldehyde reductase activity in the antennae of Helicoverpa armigera
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棉铃虫触角中醛还原酶的活性
DOI：
10.1111/imb.12084
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发表时间：
2014-06-01
影响因子：
2.6
通讯作者：
Wang, C-Z.
中科院分区：
文献类型：
--
作者：
Guo, H.;Del Corso, A.;Wang, C-Z.
在本研究中，我们鉴定了 Helicoverpa 物种触角中的两种醛还原酶活性，NADH 和 NADPH 依赖性活性。我们表达了棉铃虫的醛酮还原酶（AKR）蛋白之一，它与牛醛糖还原酶有 56% 的同一性，显示出 NADPH 依赖性活性，主要在成虫的触角中表达。整体免疫染色显示该酶集中在化学感受器基部和神经的细胞中。棉铃虫AKR的酶活性与哺乳动物酶明显不同。最好的底物是 8-10 个碳原子的直链脂肪醛，但不是羟基醛。棉铃虫的两种信息素成分都是 16 个碳的不饱和醛，是非常差的底物。与哺乳动物 AKR 不同，棉铃虫酶受常见抑制剂的影响较弱，并且表现出与硫醇作用不同的行为。该酶的模型表明四个半胱氨酸处于还原形式，哺乳动物酶的七个半胱氨酸也是如此。在其他不使用醛作为信息素的昆虫物种中出现直系同源蛋白质，排除了将该酶归类为信息素降解酶的可能性，正如之前在其他昆虫物种中所描述的那样。
In the present study, we identified two aldehyde reductase activities in the antennae of Helicoverpa species, NADH and NADPH-dependent activity. We expressed one of these proteins of H.armigera, aldo-keto reductase (AKR), which bears 56% identity to bovine aldose reductase, displays a NADPH-dependent activity and is mainly expressed in the antennae of adults. Whole-mount immunostaining showed that the enzyme is concentrated in the cells at the base of chemosensilla and in the nerves. The enzyme activity of H.armigeraAKR is markedly different from those of mammalian enzymes. The best substrates are linear aliphatic aldehydes of 8-10 carbon atoms, but not hydroxyaldehydes. Both pheromone components of H.armigera, which are unsaturated aldehydes of 16 carbons, are very poor substrates. Unlike mammalian AKRs, the H.armigera enzyme is weakly affected by common inhibitors and exhibits a different behaviour from the action of thiols. A model of the enzyme suggests that the four cysteines are in their reduced form, as are the seven cysteines of mammalian enzymes. The occurrence of orthologous proteins in other insect species, that do not use aldehydes as pheromones, excludes the possibility of classifying this enzyme among the pheromone-degrading enzymes, as has been previously described in other insect species.