Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve

	Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve
	Liu, Helu 1,2; Zheng, Huaiping 1,2; Wang, Shuqi 1,2; Wang, Yajun 1,2; Li, Shengkang 1,2; Liu, Wenhua 1,2; Zhang, Guofan 3
刊名	AQUACULTURE
	2013-12-05
卷号	416 页码:146-151
关键词	Chlamys nobilis ELOVL Fatty acyl biosynthesis PUFA Bivalve
ISSN号	0044-8486
通讯作者	Zheng, HP
中文摘要	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.
英文摘要	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.
学科主题	Fisheries ; Marine & Freshwater Biology
WOS标题词	Science & Technology ; Life Sciences & Biomedicine
类目[WOS]	Fisheries ; Marine & Freshwater Biology
研究领域[WOS]	Fisheries ; Marine & Freshwater Biology
关键词[WOS]	CRASSOSTREA-VIRGINICA ; MOLECULAR-CLONING ; ATLANTIC SALMON ; ALGAL DIETS ; BIOSYNTHESIS ; IDENTIFICATION ; METABOLISM ; OYSTER ; DESATURASE ; EXPRESSION
收录类别	SCI
原文出处	10.1016/j.aquaculture.2013.09.015
语种	英语
WOS记录号	WOS:000326823000021
公开日期	2014-07-17
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/16689]
专题	海洋研究所_海洋生物技术研发中心
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.,...&Zhang, Guofan.(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.