| Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve | |
| Liu, Helu1,2; Zheng, Huaiping1,2; Wang, Shuqi1,2; Wang, Yajun1,2; Li, Shengkang1,2; Liu, Wenhua1,2; Zhang, Guofan3; Zheng, HP | |
| 2013-12-05 | |
| 发表期刊 | AQUACULTURE
 |
| ISSN | 0044-8486 |
| 卷号 | 416页码:146-151 |
| 文章类型 | Article |
| 摘要 | Enzymes that lengthen the carbon chain of polyunsaturated fatty acids (PUFAs) are keys to the biosynthesis of the highly unsaturated fatty acids. Here we report on the molecular cloning and functional characterization of a cDNA encoding a putative elongase of very long-chain fatty acids (ELOVL), a critical enzyme that catalyses the elongation of fatty acids (FAs) including PUFAs. The full length cDNA of the fatty acyl elongase from the noble scallop Chlamys nobilis was isolated by Rapid Amplification of cDNA Ends (RACE). The amplified cDNAs encoded a putative open reading frame (ORF) of 307 amino acids that contained histidine box HXXHH motif conserved in all elongases. Phylogenetic analysis suggested that the putative elongase was placed in the same group with ELOVL2 and ELOVL5, which had been demonstrated to be critical enzymes participating in the biosynthesis of PUFAs in vertebrates. Heterologous expression in yeast Saccharomyces cerevisiae demonstrated that the ORF encoded an elongase with the ability to lengthen n-3 and n-6 PUFA substrates with chain lengths of C18 and C20, exhibiting similar substrate specificities to vertebrate ELOVL5. Moreover, the noble scallop elongase could lengthen monounsaturated fatty acids to low activity, but not saturated fatty acids. The interesting point was that this elongase converted n-6 PUFA substrates more efficiently than their homologous n-3 substrates, suggesting that n-6 PUFAs might have particular biological significance in C. nobilis. (C) 2013 Elsevier B. V. All rights reserved.; Enzymes that lengthen the carbon chain of polyunsaturated fatty acids (PUFAs) are keys to the biosynthesis of the highly unsaturated fatty acids. Here we report on the molecular cloning and functional characterization of a cDNA encoding a putative elongase of very long-chain fatty acids (ELOVL), a critical enzyme that catalyses the elongation of fatty acids (FAs) including PUFAs. The full length cDNA of the fatty acyl elongase from the noble scallop Chlamys nobilis was isolated by Rapid Amplification of cDNA Ends (RACE). The amplified cDNAs encoded a putative open reading frame (ORF) of 307 amino acids that contained histidine box HXXHH motif conserved in all elongases. Phylogenetic analysis suggested that the putative elongase was placed in the same group with ELOVL2 and ELOVL5, which had been demonstrated to be critical enzymes participating in the biosynthesis of PUFAs in vertebrates. Heterologous expression in yeast Saccharomyces cerevisiae demonstrated that the ORF encoded an elongase with the ability to lengthen n-3 and n-6 PUFA substrates with chain lengths of C18 and C20, exhibiting similar substrate specificities to vertebrate ELOVL5. Moreover, the noble scallop elongase could lengthen monounsaturated fatty acids to low activity, but not saturated fatty acids. The interesting point was that this elongase converted n-6 PUFA substrates more efficiently than their homologous n-3 substrates, suggesting that n-6 PUFAs might have particular biological significance in C. nobilis. (C) 2013 Elsevier B. V. All rights reserved. |
| 关键词 | Chlamys Nobilis Elovl Fatty Acyl Biosynthesis Pufa Bivalve |
| 学科领域 | Fisheries ; Marine & Freshwater Biology |
| DOI | 10.1016/j.aquaculture.2013.09.015 |
| URL | 查看原文 |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS研究方向 | Fisheries ; Marine & Freshwater Biology |
| WOS类目 | Fisheries ; Marine & Freshwater Biology |
| WOS记录号 | WOS:000326823000021 |
| WOS关键词 | CRASSOSTREA-VIRGINICA ; MOLECULAR-CLONING ; ATLANTIC SALMON ; ALGAL DIETS ; BIOSYNTHESIS ; IDENTIFICATION ; METABOLISM ; OYSTER ; DESATURASE ; EXPRESSION |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 引用统计 | |
| 文献类型 | 期刊论文 |
| 条目标识符 | http://ir.qdio.ac.cn/handle/337002/16689 |
| 专题 | 海洋生物技术研发中心 |
| 通讯作者 | Zheng, HP |
| 作者单位 | 1.Shantou Univ, Key Lab Marine Biotechnol Guangdong Prov, Shantou 515063, Peoples R China 2.Mariculture Res Ctr Subtrop Shellfish & Algae, Dept Educ Guangdong Prov, Shantou 515063, Peoples R China 3.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China |
| 推荐引用方式 GB/T 7714 | Liu, Helu,Zheng, Huaiping,Wang, Shuqi,et al. Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve[J]. AQUACULTURE,2013,416:146-151. |
| APA | Liu, Helu.,Zheng, Huaiping.,Wang, Shuqi.,Wang, Yajun.,Li, Shengkang.,...&Zheng, HP.(2013).Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve.AQUACULTURE,416,146-151. |
| MLA | Liu, Helu,et al."Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve".AQUACULTURE 416(2013):146-151. |
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