scholarly journals Functional characterisation of fatty acyl desaturase, Fads2, and elongase, Elovl5, in the Boddart's goggle‐eyed goby Boleophthalmus boddarti (Gobiidae) suggests an incapacity for long‐chain polyunsaturated fatty acid biosynthesis

2020 ◽  
Vol 97 (1) ◽  
pp. 83-99
Author(s):  
Han‐Jie Soo ◽  
Ka Kei Sam ◽  
Joey Chong ◽  
Nyok‐Sean Lau ◽  
Seng Yeat Ting ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Polyunsaturated Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Fatty Acyl ◽  
Chain Polyunsaturated Fatty Acid ◽  
Acid Biosynthesis ◽  
Functional Characterisation ◽  
Fatty Acyl Desaturase ◽  
Long Chain

scholarly journals Functional characterization of fatty acyl desaturase Fads2 and Elovl5 elongase in the Boddart’s goggle-eyed goby, Boleophthalmus boddarti (Gobiidae) suggest an incapacity for long-chain polyunsaturated fatty acid biosynthesis

2019 ◽  
Author(s):  
Han-Jie Soo ◽  
Joey Chong ◽  
Lau Nyok Sean ◽  
Seng Yeat Ting ◽  
Sam Ka Kei ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Polyunsaturated Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Functional Characterization ◽  
Fatty Acyl ◽  
Chain Polyunsaturated Fatty Acid ◽  
Acid Biosynthesis ◽  
Wide Range ◽  
Fatty Acyl Desaturase ◽  
Long Chain

AbstractLong-chain polyunsaturated fatty acid biosynthesis, a process to convert C18 polyunsaturated fatty acids to eicosapentaenoic acid (EPA), docosahexaenoic acid (DHA) or arachidonic acid (ARA) requires the concerted activities of two enzymes, the fatty acyl desaturase (Fads) and elongase (Elovl). This study highlights the cloning, functional characterisation and tissue expression pattern of a Fads and Elovl from the Boddart’s goggle-eyed goby (Boleophthalmus boddarti), a mudskipper species widely distributed in the Indo-Pacific region. Phylogenetic analysis revealed that the cloned Fads and Elovl are clustered with other teleost Fads2 and Elovl5 orthologs, respectively. Interrogation of the genome of several mudskipper species, namely B. pectinirostris, Periophthalmus schlosseri and P. magnuspinnatus revealed a single Fads2 for each respective species while two elongases, Elovl5 and Elovl4 were detected. Using a heterologous yeast assay, the B. boddarti Fads2 was shown to possess low desaturation activity on C18 PUFA. In addition, there was no desaturation of C20 and C22 substrates. In comparison, the Elovl5 showed a wide range of substrate specificity, with capacity to elongate C18, C20 and C22 PUFA substrates. We identified an amino acid residue in the B. boddarti Elovl5 that affect the capacity to bind C22 PUFA substrate. Both genes are highly expressed in brain tissue. Among all tissues, DHA is highly concentrated in neuron-rich tissues while EPA is highly deposited in gills. Taken together, the results showed that due to disability of desaturation steps, B. boddarti is unable to biosynthesis LC-PUFA, relying on dietary intake to acquire these nutrients.

scholarly journals The same rat Δ6-desaturase not only acts on 18- but also on 24-carbon fatty acids in very-long-chain polyunsaturated fatty acid biosynthesis

2002 ◽  
Vol 364 (1) ◽  
pp. 49-55 ◽  
Author(s):  
Sabine D'ANDREA ◽  
Hervé GUILLOU ◽  
Sophie JAN ◽  
Daniel CATHELINE ◽  
Jean-Noël THIBAULT ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Polyunsaturated Fatty Acid ◽  
Unsaturated Fatty Acids ◽  
Fatty Acid Biosynthesis ◽  
Chain Polyunsaturated Fatty Acid ◽  
Acid Biosynthesis ◽  
Highly Unsaturated Fatty Acids ◽  
Long Chain ◽  
Δ6 Desaturase

The recently cloned Δ6-desaturase is known to catalyse the first step in very-long-chain polyunsaturated fatty acid biosynthesis, i.e. the desaturation of linoleic and α-linolenic acids. The hypothesis that this enzyme could also catalyse the terminal desaturation step, i.e. the desaturation of 24-carbon highly unsaturated fatty acids, has never been elucidated. To test this hypothesis, the activity of rat Δ6-desaturase expressed in COS-7 cells was investigated. Recombinant Δ6-desaturase expression was analysed by Western blot, revealing a single band at 45kDa. The putative involvement of this enzyme in the Δ6-desaturation of C24:5n-3 to C24:6n-3 was measured by incubating transfected cells with C22:5n-3. Whereas both transfected and non-transfected COS-7 cells were able to synthesize C24:5n-3 by elongation of C22:5n-3, only cells expressing Δ6-desaturase were also able to produce C24:6n-3. In addition, Δ6-desaturation of [1-14C]C24:5n-3 was assayed invitro in homogenates from COS-7 cells expressing Δ6-desaturase or not, showing that Δ6-desaturase catalyses the conversion of C24:5n-3 to C24:6n-3. Evidence is therefore presented that the same rat Δ6-desaturase catalyses not only the conversion of C18:3n-3 to C18:4n-3, but also the conversion of C24:5n-3 to C24:6n-3. A similar mechanism in the n-6 series is strongly suggested.

Sign in / Sign up

Export Citation Format

Share Document