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Unique fatty acid desaturase capacities uncovered in Hediste diversicolor illustrate the roles of aquatic invertebrates in trophic upgrading

AuthorsKabeya, Naoki; Gür, İbrahim; Oboh, Angela; Ove Evjemo, Jan; Malzahn, Arne M.; Hontoria, Francisco ; Navarro, Juan Carlos ; Monroig, Óscar
Methyl-end desaturase
N-3 long-chain PUFA
Issue Date3-Aug-2020
PublisherRoyal Society (Great Britain)
CitationPhilosophical Transactions - B - Biological Sciences 375:1804 (2020)
AbstractOmega-3 (ω3 or n-3) long-chain polyunsaturated fatty acids (PUFA) including eicosapentaenoic acid and docosahexaenoic acid (DHA), play physiologically important roles in vertebrates. These compounds have long been believed to be originated almost exclusively from aquatic (mostly marine) single-cell organisms. Yet, a recent study has discovered that many invertebrates possess a type of enzymes called methyl-end desaturases (ωx) that enables them to endogenously produce n-3 long-chain PUFA and could make a significant contribution to production of these compounds in the marine environment. Polychaetes are major components of benthic fauna and thus important to maintain a robust food web as a recycler of organic matter and a prey item for higher trophic level species like fish. In the present study, we investigated the ωx enzymes from the common ragworm Hediste diversicolor, a common inhabitant in sedimentary littoral ecosystems of the North Atlantic. Functional assays of the H. diversicolor ωx demonstrated unique desaturation capacities. An ω3 desaturase mediated the conversion of n-6 fatty acid substrates into their corresponding n-3 products including DHA. A further enzyme possessed unique regioselectivities combining both ω6 and ω3 desaturase activities. These results illustrate that the long-chain PUFA biosynthetic enzymatic machinery of aquatic invertebrates such as polychaetes is highly diverse and clarify that invertebrates can be major contributors to fatty acid trophic upgrading in aquatic food webs.
Publisher version (URL)http://dx.doi.org/10.1098/rstb.2019.0654
Appears in Collections:(IATS) Artículos
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