Please use this identifier to cite or link to this item: http://hdl.handle.net/1893/20566
Appears in Collections:Aquaculture Journal Articles
Peer Review Status: Refereed
Title: Diversification of substrate specificities in teleostei Fads2: characterization of Δ4 and Δ6Δ5 desaturases of Chirostoma estor
Authors: Fonseca-Madrigal, Jorge
Navarro, Juan Carlos
Hontoria, Francisco
Tocher, Douglas R
Martinez-Palacios, Carlos A
Monroig, Oscar
Contact Email: drt1@stir.ac.uk
Keywords: biosynthesis
elongase of very long-chain fatty acids
evolution
fatty acyl desaturases
long- chain polyunsaturated fatty acids
teleosts.
Issue Date: Jul-2014
Publisher: American Society for Biochemistry and Molecular Biology
Citation: Fonseca-Madrigal J, Navarro JC, Hontoria F, Tocher DR, Martinez-Palacios CA & Monroig O (2014) Diversification of substrate specificities in teleostei Fads2: characterization of Δ4 and Δ6Δ5 desaturases of Chirostoma estor, Journal of Lipid Research, 55 (7), pp. 1408-1419.
Abstract: Currently existing data show that the capability for long-chain PUFA (LC-PUFA) biosynthesis in teleost fish is more diverse than in other vertebrates. Such diversity has been primarily linked to the subfunctionalization that teleostei fatty acyl desaturase (Fads)2 desaturases have undergone during evolution. We previously showed that Chirostoma estor, one of the few representatives of freshwater atherinopsids, had the ability for LC-PUFA biosynthesis from C18 PUFA precursors, in agreement with this species having unusually high contents of DHA. The particular ancestry and pattern of LC-PUFA biosynthesis activity of C. estor make this species an excellent model for study to gain further insight into LC-PUFA biosynthetic abilities among teleosts. The present study aimed to characterize cDNA sequences encoding fatty acyl elongases and desaturases, key genes involved in the LC-PUFA biosynthesis. Results show that C. estor expresses an elongase of very long-chain FA (Elovl)5 elongase and two Fads2 desaturases displaying Δ4 and Δ6/Δ5 specificities, thus allowing us to conclude that these three genes cover all the enzymatic abilities required for LC-PUFA biosynthesis from C18 PUFA. In addition, the specificities of the C. estor Fads2 enabled us to propose potential evolutionary patterns and mechanisms for subfunctionalization of Fads2 among fish lineages.
Type: Journal Article
URI: http://hdl.handle.net/1893/20566
DOI Link: http://dx.doi.org/10.1194/jlr.M049791
Rights: This research was originally published in Journal of Lipid Research. Fonseca-Madrigal J, Navarro JC, Hontoria F, Tocher DR, Martinez-Palacios CA & Monroig O (2014) Diversification of substrate specificities in teleostei Fads2: characterization of Δ4 and Δ6Δ5 desaturases of Chirostoma estor, The Journal of Lipid Research, 55 (7), pp. 1408-1419 © the American Society for Biochemistry and Molecular Biology
Affiliation: Michoacan University of San Nicolas de Hildalgo (UMSNH)
Institute of Aquaculture Torre de la Sal
Institute of Aquaculture Torre de la Sal
Aquaculture
Michoacan University of San Nicolas de Hildalgo (UMSNH)
Complex Systems

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