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Cloning and functional characterisation of polyunsaturated fatty acid elongases of marine and freshwater teleost fish.

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 alpha-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.

Authors+Show Affiliations

Institute of Aquaculture, University of Stirling, Stirling FK9 4LA, Scotland, United Kingdom.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16183312

Citation

Agaba, Morris K., et al. "Cloning and Functional Characterisation of Polyunsaturated Fatty Acid Elongases of Marine and Freshwater Teleost Fish." Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, vol. 142, no. 3, 2005, pp. 342-52.
Agaba MK, Tocher DR, Zheng X, et al. Cloning and functional characterisation of polyunsaturated fatty acid elongases of marine and freshwater teleost fish. Comp Biochem Physiol B, Biochem Mol Biol. 2005;142(3):342-52.
Agaba, M. K., Tocher, D. R., Zheng, X., Dickson, C. A., Dick, J. R., & Teale, A. J. (2005). Cloning and functional characterisation of polyunsaturated fatty acid elongases of marine and freshwater teleost fish. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 142(3), pp. 342-52.
Agaba MK, et al. Cloning and Functional Characterisation of Polyunsaturated Fatty Acid Elongases of Marine and Freshwater Teleost Fish. Comp Biochem Physiol B, Biochem Mol Biol. 2005;142(3):342-52. PubMed PMID: 16183312.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cloning and functional characterisation of polyunsaturated fatty acid elongases of marine and freshwater teleost fish. AU - Agaba,Morris K, AU - Tocher,Douglas R, AU - Zheng,Xiaozhong, AU - Dickson,Cathryn A, AU - Dick,James R, AU - Teale,Alan J, Y1 - 2005/09/23/ PY - 2005/05/27/received PY - 2005/08/22/revised PY - 2005/08/24/accepted PY - 2005/9/27/pubmed PY - 2006/1/6/medline PY - 2005/9/27/entrez SP - 342 EP - 52 JF - Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology JO - Comp. Biochem. Physiol. B, Biochem. Mol. Biol. VL - 142 IS - 3 N2 - 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 alpha-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. SN - 1096-4959 UR - https://www.unboundmedicine.com/medline/citation/16183312/Cloning_and_functional_characterisation_of_polyunsaturated_fatty_acid_elongases_of_marine_and_freshwater_teleost_fish_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1096-4959(05)00199-5 DB - PRIME DP - Unbound Medicine ER -