Biosynthesis of essential fatty acids in Octopus vulgaris (Cuvier, 1797): Molecular cloning, functional characterisation and tissue distribution of a fatty acyl elongase
Biosynthesis of essential fatty acids in Octopus vulgaris (Cuvier, 1797): Molecular cloning, functional characterisation and tissue distribution of a fatty acyl elongase
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DOI：
10.1016/j.aquaculture.2012.07.016
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发表时间：
2012-09
期刊：
影响因子：
4.5
通讯作者：
Ó. Monroig;D. Guinot;F. Hontoria;D. Tocher;J. Navarro
中科院分区：
文献类型：
--
作者：
Ó. Monroig;D. Guinot;F. Hontoria;D. Tocher;J. Navarro
多不饱和脂肪酸（PUFAs）已被确定为普通章鱼（Octopus vulgaris）的关键营养素，特别是对于其早期生命周期阶段（Octopus vulgaris）。我们的首要目标是确定膳食必需脂肪酸（FA）的章鱼的内源性PUFA生物合成途径的酶的特性。在这里，我们报告的分子克隆和功能特性的cDNA编码的推定的延伸酶的非常长链脂肪酸（Elovl），一个关键的酶，催化延长FA，包括PUFA。我们的研究结果表明，章鱼Elovl与Elovl 5和Elovl 2，这两种延伸酶在脊椎动物中的PUFA生物合成中具有已证实的作用，在遗传学上相关。支持章鱼Elovl在PUFA生物合成中的作用的进一步证据通过其在酵母中的活性的功能表征来提供。证实章鱼Elovl的表达赋予酵母延长一些C18和C20 PUFA的能力，而C22 PUFA底物保持未修饰。因此，章鱼延伸酶表现出的底物特异性与脊椎动物Elov 15的底物特异性一致。有趣的是，章鱼Elovl延长n-6 PUFA底物的效率高于其同源的n-3底物，这表明n-6 PUFA可能在O.普通的最后，我们研究了新克隆的Elovl在非亚甲基中断的FA的生物合成中的潜在作用，该化合物通常存在于海洋无脊椎动物中，并被证实也存在于普通章鱼中。
Polyunsaturated fatty acids (PUFAs) have been identified as key nutrients for the common octopus (Octopus vulgaris), particularly for its early life-cycle stages (paralarvae). Our overarching aim is to identify the dietary essential fatty acid (FA) for octopus paralarvae through characterisation of the enzymes of endogenous PUFA biosynthetic pathways. Here we report on the molecular cloning and functional characterisation of a cDNA encoding a putative elongase of very long-chain fatty acids (Elovl), a critical enzyme that catalyses the elongation of FA including PUFA. Our results suggest that the octopus Elovl is phylogenetically related to Elovl5 and Elovl2, two elongases with demonstrated roles in PUFA biosynthesis in vertebrates. Further evidence supporting a role of the octopus Elovl in PUFA biosynthesis was provided through functional characterisation of its activity in yeast. It was confirmed that expression of the octopus Elovl conferred on yeast the ability to elongate some C18 and C20 PUFAs, while C22 PUFA substrates remained unmodified. Therefore, the substrate specificities exhibited by the octopus elongase were consistent with those of vertebrate Elovl5. Interestingly, the octopus Elovl elongated n−6 PUFA substrates more efficiently than their homologous n−3 substrates, suggesting that n−6 PUFA may have particular biological significance in O. vulgaris. Finally, we investigated the potential role of the newly cloned Elovl in the biosynthesis of non-methylene-interrupted FA, compounds typically found in marine invertebrates and confirmed to be also present in the common octopus.