Identification and functional characterization of polyunsaturated fatty acid elongase (McELOVL5) gene from pike eel (Muraenesox cinereus)

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• 作者：Sun Hee Kim (1)
  So Yun Kim (1)
  Eui Ki Kim (4)
  Kyung Hee Roh (1)
  Jung-Bong Kim (1)
  Kwang-Soo Kim (2)
  Hyun Uk Kim (1)
  Kyeong-Ryeol Lee (1)
  Han-Chul Kang (1)
  Jong-Sug Park (3)
  Kyung Hyun Kim (4)
  Jong-Bum Kim (1)
  
• 关键词：Fatty acid elongase ; Muraenesox cinereus ; Pik eel ; Polyunsaturated fatty acid elongase ; Saccharomyces cerevisiae
• 刊名：Biotechnology Letters
• 出版年：2014
• 出版时间：January 2014
• 年：2014
• 卷：36
• 期：1
• 页码：29-37
• 全文大小：650 KB
• 作者单位：Sun Hee Kim (1)
  So Yun Kim (1)
  Eui Ki Kim (4)
  Kyung Hee Roh (1)
  Jung-Bong Kim (1)
  Kwang-Soo Kim (2)
  Hyun Uk Kim (1)
  Kyeong-Ryeol Lee (1)
  Han-Chul Kang (1)
  Jong-Sug Park (3)
  Kyung Hyun Kim (4)
  Jong-Bum Kim (1)
  
  1. National Academy of Agricultural Science, Rural Development Administration, Seodun-Dong, Suwon, 441-707, Korea
  4. Department of Biotechnology & Bioinformatics, Korea University, Rm 244, Life Science & Biotechnology (Nokji), Anam dong, Sungbuk gu, Seoul, 136-701, Korea
  2. National Institute of Crop Science, Rural Development Administration, Seodun-Dong, Suwon, 441-707, Korea
  3. R&D Coordination Division, Rural Development Administration, Seodun-Dong, Suwon, 441-707, Korea
  
• ISSN：1573-6776

文摘

The cDNA coding for a polyunsaturated fatty acid elongase (McELOVL5) was isolated from the brain of the pike eel (Muraenesox cinereus) being based on available sequences in 23 types of fish. Four sequence variants were identified with different amino acid substitutions as compared with two clones of McELOVL5 gene (McELOVL5 11.7 and McELOVL5 12.4). When the two variants of McELOVL5 were expressed in Saccharomyces cerevisiae, the two recombinant yeasts elongated γ-linolenic acid (GLA, 18:3n-6) to di-homo-γ-linolenic acid (DGLA, 20:3n-6) but differed in the rate of GLA conversion to DGLA. Cells transformed with McELOVL5 12.4 also converted arachidonic acid (20:4n-6) and eicosapentaenoic acid (20:5n-3) to docosatetraenoic acid (22:4n-6) and docosapentaenoic acid (22:5n-3), respectively. However McELOVL5 11.7 lost its function for the elongation of C20 fatty acids. The four sequence variants have changed substrate specificities. Three-dimensional models of the McELOVL5 proteins are suggested.