Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve
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 c...
Published in: | Aquaculture |
---|---|
Main Authors: | , , , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
2013
|
Subjects: | |
Online Access: | http://ir.qdio.ac.cn/handle/337002/16689 https://doi.org/10.1016/j.aquaculture.2013.09.015 |
id |
ftchinacasciocas:oai:ir.qdio.ac.cn:337002/16689 |
---|---|
record_format |
openpolar |
spelling |
ftchinacasciocas:oai:ir.qdio.ac.cn:337002/16689 2023-05-15T15:33:01+02:00 Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve Liu, Helu Zheng, Huaiping Wang, Shuqi Wang, Yajun Li, Shengkang Liu, Wenhua Zhang, Guofan Zheng, HP 2013-12-05 http://ir.qdio.ac.cn/handle/337002/16689 https://doi.org/10.1016/j.aquaculture.2013.09.015 英语 eng AQUACULTURE Liu, Helu; Zheng, Huaiping; Wang, Shuqi; Wang, Yajun; Li, Shengkang; Liu, Wenhua; Zhang, Guofan.Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve,AQUACULTURE,2013,416():146-151 http://ir.qdio.ac.cn/handle/337002/16689 doi:10.1016/j.aquaculture.2013.09.015 6 Chlamys Nobilis Elovl Fatty Acyl Biosynthesis Pufa Bivalve Fisheries Marine & Freshwater Biology Science & Technology Life Sciences & Biomedicine CRASSOSTREA-VIRGINICA MOLECULAR-CLONING ATLANTIC SALMON ALGAL DIETS BIOSYNTHESIS IDENTIFICATION METABOLISM OYSTER DESATURASE EXPRESSION Article 期刊论文 2013 ftchinacasciocas https://doi.org/10.1016/j.aquaculture.2013.09.015 2022-06-27T05:35:44Z 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 ... Article in Journal/Newspaper Atlantic salmon Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR Aquaculture 416-417 146 151 |
institution |
Open Polar |
collection |
Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR |
op_collection_id |
ftchinacasciocas |
language |
English |
topic |
Chlamys Nobilis Elovl Fatty Acyl Biosynthesis Pufa Bivalve Fisheries Marine & Freshwater Biology Science & Technology Life Sciences & Biomedicine CRASSOSTREA-VIRGINICA MOLECULAR-CLONING ATLANTIC SALMON ALGAL DIETS BIOSYNTHESIS IDENTIFICATION METABOLISM OYSTER DESATURASE EXPRESSION |
spellingShingle |
Chlamys Nobilis Elovl Fatty Acyl Biosynthesis Pufa Bivalve Fisheries Marine & Freshwater Biology Science & Technology Life Sciences & Biomedicine CRASSOSTREA-VIRGINICA MOLECULAR-CLONING ATLANTIC SALMON ALGAL DIETS BIOSYNTHESIS IDENTIFICATION METABOLISM OYSTER DESATURASE EXPRESSION Liu, Helu Zheng, Huaiping Wang, Shuqi Wang, Yajun Li, Shengkang Liu, Wenhua Zhang, Guofan Zheng, HP Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve |
topic_facet |
Chlamys Nobilis Elovl Fatty Acyl Biosynthesis Pufa Bivalve Fisheries Marine & Freshwater Biology Science & Technology Life Sciences & Biomedicine CRASSOSTREA-VIRGINICA MOLECULAR-CLONING ATLANTIC SALMON ALGAL DIETS BIOSYNTHESIS IDENTIFICATION METABOLISM OYSTER DESATURASE EXPRESSION |
description |
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 ... |
format |
Article in Journal/Newspaper |
author |
Liu, Helu Zheng, Huaiping Wang, Shuqi Wang, Yajun Li, Shengkang Liu, Wenhua Zhang, Guofan Zheng, HP |
author_facet |
Liu, Helu Zheng, Huaiping Wang, Shuqi Wang, Yajun Li, Shengkang Liu, Wenhua Zhang, Guofan Zheng, HP |
author_sort |
Liu, Helu |
title |
Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve |
title_short |
Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve |
title_full |
Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve |
title_fullStr |
Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve |
title_full_unstemmed |
Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve |
title_sort |
cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop chlamys nobilis reeve |
publishDate |
2013 |
url |
http://ir.qdio.ac.cn/handle/337002/16689 https://doi.org/10.1016/j.aquaculture.2013.09.015 |
genre |
Atlantic salmon |
genre_facet |
Atlantic salmon |
op_relation |
AQUACULTURE Liu, Helu; Zheng, Huaiping; Wang, Shuqi; Wang, Yajun; Li, Shengkang; Liu, Wenhua; Zhang, Guofan.Cloning and functional characterization of a polyunsaturated fatty acid elongase in a marine bivalve noble scallop Chlamys nobilis Reeve,AQUACULTURE,2013,416():146-151 http://ir.qdio.ac.cn/handle/337002/16689 doi:10.1016/j.aquaculture.2013.09.015 |
op_rights |
6 |
op_doi |
https://doi.org/10.1016/j.aquaculture.2013.09.015 |
container_title |
Aquaculture |
container_volume |
416-417 |
container_start_page |
146 |
op_container_end_page |
151 |
_version_ |
1766363489720336384 |