| Title | Isolation and Functional Characterization of a Delta 6-Desaturase Gene from the Pike Eel (Muraenesox cinereus) |
|---|---|
| Author | Sun Hee Kim1, Kyung Hee Roh1, Jung-Bong Kim1, Kwang-Soo Kim2, Nam Shin Kim3, Hyun Uk Kim1, Kyeong-Ryeol Lee1, Jong-Sug Park4, and Jong-Bum Kim1* |
| Address | 1National Academy of Agricultural Science, Rural Development Administration, Suwon 441-707, Republic of Korea, 2National Institute of Crop Science, Rural Development Administration, Suwon 441-707, Republic of Korea, 3Korean Bioinformation Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Republic of Korea, 4R&D Coordination Division, Rural Development Administration, Suwon 441-707, Republic of Korea |
| Bibliography | Journal of Microbiology, 51(6),807–813, 2013, |
| DOI | 10.1007/s12275-013-3144-3 |
| Key Words | delta 6-desaturase, γ-linolenic acid, Muraenesox cinereus, Saccharomyces cerevisiae, stearidonic acid |
| Abstract | Stearidonic acid (STA; 18:4n-3) and γ-linolenic acid (GLA; 18:3n-6) are significant intermediates in the biosynthetic pathway for the very-long-chain polyunsaturated fatty acids of eicosapentaenoic acid (EPA; 20:5n-3) and arachidonic acid (ARA; 20:4n-6), respectively. To develop a sustainable system for the production of dietary polyunsaturated fatty acids, we focused on the action of the enzyme delta 6-desaturase (D6DES) on the essential acids, linoleic acid (LA; 18:2n-6) and α-linolenic acid (ALA; 18:3n-3). A 1,335-bp full-length cDNA encoding D6DES (McD6DES) was cloned from Muraenesox cinereus using degenerate PCR and RACE-PCR methods. To investigate the enzymatic activity of McD6DES in the production of n-6 and n-3 fatty acids, a recombinant plasmid expressing McD6DES (pYES-McD6DES) was transformed into and expressed in Saccharomyces cerevisiae. The exogenously expressed McD6DES produced GLA and STA at conversion rates of 14.2% and 45.9%, respectively, from the exogenous LA and ALA substrates. These results indicate that McD6DES is essentially a delta 6-desaturase involved in very-long-chain polyunsaturated fatty acid synthesis. |