|Appears in Collections:||Aquaculture Journal Articles|
|Peer Review Status:||Refereed|
|Title:||Cloning and functional characterisation of polyunsaturated fatty acid elongases of marine and freshwater teleost fish|
|Authors:||Agaba, Morris K|
Tocher, Douglas R
Dick, James R
Teale, Alan J
|Keywords:||Fatty acyl elongases|
|Citation:||Agaba MK, Tocher DR, Zheng X, Dickson C, Dick JR & Teale AJ (2005) Cloning and functional characterisation of polyunsaturated fatty acid elongases of marine and freshwater teleost fish, Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology, 142 (3), pp. 342-352.|
|Abstract:||Enzymes that lengthen the carbon chain of polyunsaturated fatty acids are key to the biosynthesis of the highly unsaturated fatty acids, arachidonic, eicosapentaenoic and docosahexaenoic acids from linoleic and α-linolenic acids. A Mortierella alpina cDNA polyunsaturated fatty acid elongase sequence identified mammalian, amphibian, zebrafish and insect expressed sequence tags (ESTs) in GenBank. Consensus primers were designed in conserved motifs and used to isolate full length cDNA from livers of several fish species by Rapid Amplification of cDNA Ends (RACE). The amplified cDNAs encoded putative open reading frames (ORFs) of 288-294 amino acids that were highly conserved among the fish species. Heterologous expression in yeast, Saccharomyces cerevisiae, demonstrated that all of the ORFs encoded elongases with the ability to lengthen polyunsaturated fatty acid substrates with chain lengths from C18 to C22 and also monounsaturated fatty acids, but not saturated fatty acids. There were differences in the functional competence of the elongases from different fish species. Most of the fish elongases showed a pattern of activity towards different fatty acid substrates in the rank order C18 > C20 >C22, although the tilapia and turbot elongases had similar activity towards 18:4n-3 and 20:5n-3. The fish elongases generally showed greater activity or similar activities with n-3 than with n-6 homologues, with the exception of the cod enzyme which was more active towards n-6 fatty acids.|
|Rights:||Published in Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology by Elsevier. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, Volume 142, Issue 3, November 2005, pp. 342 - 352.; This is the peer reviewed version of this article.; NOTICE: this is the author’s version of a work that was accepted for publication in Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, VOL 142, ISSUE 3, (November 2005). DOI 10.1016/j.cbpb.2005.08.005.|
|Affiliation:||University of Stirling|
University of Stirling
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