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Appears in Collections:Aquaculture Journal Articles
Peer Review Status: Refereed
Title: Zebrafish cDNA encoding multifunctional fatty acid elongase involved in production of eicosapentaenoic (20:5n-3) and docosahexaenoic (22:6n-3) acids
Authors: Agaba, Morris K
Tocher, Douglas R
Dickson, Cathryn
Dick, James R
Teale, Alan J
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Keywords: Fatty acyl elongases
Danio rerio
cDNA cloning
Functional characterisation
Issue Date: Jun-2004
Publisher: Springer
Citation: Agaba MK, Tocher DR, Dickson C, Dick JR & Teale AJ (2004) Zebrafish cDNA encoding multifunctional fatty acid elongase involved in production of eicosapentaenoic (20:5n-3) and docosahexaenoic (22:6n-3) acids, Marine Biotechnology, 6 (3), pp. 251-261.
Abstract: Enzymes that increase the chain length of fatty acids are essential for biosynthesis of highly unsaturated fatty acids. The gLELO gene encodes a protein involved in the elongation of polyunsaturated fatty acids in the fungus Mortierella alpina. A search of the Genbank database identified several EST sequences, including one obtained from zebrafish (Danio rerio), with high similarity to gLELO. The full-length transcript, ZfELO, encoding a polypeptide of 291 amino acid residues was isolated from zebrafish liver cDNA. The predicted amino acid sequence of the open reading frame (ORF) shared high similarity with the elongases of C. elegans and human. When expressed in Saccharomyces cerevisiae, the zebrafish ORF conferred the ability to lengthen the chain of a range of C18, C20 and C22 polyunsaturated fatty acids, indicating that biosynthesis of 22:6n-3 from 18:3n-3 via a 24-carbon intermediate is not only feasible, but that one elongase enzyme can perform all three elongation steps required. The zebrafish enzyme was also able to elongate monounsaturated and saturated fatty acids, and thus demonstrates a greater level of promiscuity in terms of substrate use than any elongase enzyme described previously.
Type: Journal Article
DOI Link:
Rights: Published in Marine Biotechnology by Springer.; The final publication is available at
Affiliation: University of Stirling
University of Stirling

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