Comparative and functional analysis of desaturase FADS1 (∆5) and FADS2 (∆6) orthologues of marine organisms.

Fatty acid desaturases are key enzymes involved in unsaturated fatty acid biosynthesis, which insert double bonds at specific positions of fatty acids, playing a pivotal role in unsaturated fatty acid synthesis required for membrane lipid fluidity. The ∆5 and ∆6 desaturases are responsible for producing long chain-polyunsaturated fatty acids (LC-PUFA) through their precursors α-linolenic acid and linoleic acid in organisms lacking or with very low ability to synthesize LC-PUFA by themselves. Extensive studies of fatty acid desaturases are available in model organisms, such as humans and mouse; however, the diversity of these genes in the marine biodiversity is less known. This study performed an exhaustive analysis to identify the ∆5 and ∆6 desaturases in the available marine genomes in databases, as well as transcriptomes and EST databases, and their coding sequences were compared to the well-characterized ∆5 and ∆6 desaturases from humans. The FADS1 and FADS2 genetic structures are well conserved among all the organisms analyzed. A common amino acid pattern was identified to discriminate between ∆5 and ∆6 desaturases. The analysis of the conserved motif involved in catalysis showed that 20% of the desaturases, ∆5 and ∆6, have lost motifs required for catalysis. Additionally, bifunctional ∆5/∆6 desaturases were able to be identified by amino acid sequence patterns found in previously described enzymes. A revision of the expression profiles and functional activity on sequences in databases and scientific literature provided information regarding the function of these marine organism enzymes.
Competing Interests: Declaration of competing interest The authors declare that there is no conflict of interest.
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