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

Authors
Kim, Sun HeeKim, So YunKim, Eui KiRoh, Kyung HeeKim, Jung-BongKim, Kwang-SooKim, Hyun UkLee, Kyeong-RyeolKang, Han-ChulPark, Jong-SugKim, Kyung HyunKim, Jong-Bum
Issue Date
1월-2014
Publisher
SPRINGER
Keywords
Fatty acid elongase; Muraenesox cinereus; Pik eel; Polyunsaturated fatty acid elongase; Saccharomyces cerevisiae
Citation
BIOTECHNOLOGY LETTERS, v.36, no.1, pp.29 - 37
Indexed
SCIE
SCOPUS
Journal Title
BIOTECHNOLOGY LETTERS
Volume
36
Number
1
Start Page
29
End Page
37
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/99616
DOI
10.1007/s10529-013-1344-x
ISSN
0141-5492
Abstract
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 gamma-linolenic acid (GLA, 18:3n-6) to di-homo-gamma-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 C-20 fatty acids. The four sequence variants have changed substrate specificities. Three-dimensional models of the McELOVL5 proteins are suggested.
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