1. Comparative and functional analysis of desaturase FADS1 (∆5) and FADS2 (∆6) orthologues of marine organisms.
- Author
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Rivera-Pérez C, Valenzuela-Quiñonez F, and Caraveo-Patiño J
- Subjects
- Amino Acid Sequence, Animals, Aquatic Organisms chemistry, Aquatic Organisms genetics, Aquatic Organisms metabolism, Conserved Sequence, Delta-5 Fatty Acid Desaturase, Fatty Acid Desaturases chemistry, Fatty Acid Desaturases metabolism, Fatty Acids, Unsaturated genetics, Fatty Acids, Unsaturated metabolism, Fish Proteins chemistry, Fish Proteins metabolism, Fishes metabolism, Humans, Fatty Acid Desaturases genetics, Fish Proteins genetics, Fishes genetics, Genomics, Transcriptome
- Abstract
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., (Copyright © 2020 Elsevier Inc. All rights reserved.)
- Published
- 2020
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