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Type: Journal article
Title: An alternative n-3 fatty acid elongation pathway utilising 18:3n-3 in barramundi (Lates calcarifer)
Author: Tu, W.
Muhlhausler, B.
James, M.
Stone, D.
Gibson, R.
Citation: Biochemical and Biophysical Research Communications, 2012; 423(1):176-182
Publisher: Academic Press Inc
Issue Date: 2012
ISSN: 0006-291X
Statement of
Wei-Chun Tu, Beverly S. Mühlhäusler, Michael J. James, David A. J. Stone, Robert A. Gibson
Abstract: Desaturase and elongase are two key enzyme categories in the long-chain polyunsaturated fatty acid (LCPUFA) pathway that convert dietary α-linolenic acid (18:3n-3) to docosahexaenoic acid (22:6n-3). The Δ6 desaturase is considered as rate limiting in the conversion. In a previous study in barramundi we demonstrated that the desaturase had a low Δ6 activity but noted that the enzyme also possessed Δ8 ability that utilised 20-carbon fatty acids. This observation suggests that an alternative pathway may exist in the barramundi via elongases to form 20-carbon metabolites from 18:3n-3 to 20:3n-3 and then Δ6/8 desaturase to 20:4n-3. Cloning of the barramundi elongation of very long-chain fatty acid gene (ELOVL) and heterologous expression of the corresponding elongase were performed to examine activity with regard to time course, substrate concentration and substrate preference. Results revealed that the barramundi elongase showed a broad range of substrate specificity including 18-carbon PUFA (including 18:3n-3 and 18:2n-6), 20- and 22-carbon LCPUFA, with greater activity towards omega-3 (n-3) than n-6 fatty acids. The findings from this study provide molecular evidence for an alternative n-3 fatty acid elongation pathway utilising 18:3n-3 in barramundi.
Keywords: α-Linolenic acid (18:3n-3); Elongase; ELOVL; Heterologous expression; LCPUFA metabolism
Rights: © 2012 Elsevier Inc. All rights reserved.
RMID: 0020121558
DOI: 10.1016/j.bbrc.2012.05.110
Appears in Collections:Agriculture, Food and Wine publications

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