Cloning and molecular characterization of a delta-6 fatty acid desaturase gene from Isochrysis sp. CCMM5001

2015 ◽  
Vol 28 (2) ◽  
pp. 921-929 ◽  
Author(s):  
Shuai Wang ◽  
Li Zheng ◽  
Zhisong Cui ◽  
Junhui Chen ◽  
Baijuan Yang ◽  
...  
FEBS Letters ◽  
2004 ◽  
Vol 573 (1-3) ◽  
pp. 45-50 ◽  
Author(s):  
Dongsheng Wei ◽  
Mingchun Li ◽  
Xinxin Zhang ◽  
Yong Ren ◽  
Laijun Xing

2007 ◽  
Vol 29 (6) ◽  
pp. 959-964 ◽  
Author(s):  
Bei Niu ◽  
Huaxun Ye ◽  
Ying Xu ◽  
Shenghua Wang ◽  
Peng Chen ◽  
...  

2006 ◽  
Vol 53 (4) ◽  
pp. 753-759 ◽  
Author(s):  
D Sh Wei ◽  
M Ch Li ◽  
X X Zhang ◽  
H Zhou ◽  
L J Xing

The methylotrophic yeast Pichia pastoris GS115, a widely used strain in production of various heterologous proteins, especially membrane-bound enzymes, can also produce linoleic and linolenic acids, which indicates the existence of membrane-bound Delta12 and Delta15-fatty acid desaturases. This paper describes the cloning and functional characterization of a novel Delta12-fatty acid desaturase gene from this methylotrophic yeast. The open reading frame of the gene (named Pp-FAD12) is 1263 bp in size and encodes a 420-amino-acid peptide. The deduced Pp-FAD12 protein shows high identity (50-67%) with Delta12-fatty acid desaturases from other fungi. It also shows a high identity (57%) with Delta15-fatty acid desaturase (named Sk-FAD15) from Saccharomyces kluyveri. Expression of Pp-FAD12 in polyunsaturated fatty acids non-producing yeast Saccharomyces cerevisiae demonstrated that its product converted oleic acid (18 : 1) to linoleic acid (18 : 2). This result suggests that Pp-FAD12 encodes a novel Delta12-fatty acid desaturase in P. pastoris GS115. This is the first report about the cloning and functional characterization of Delta12-fatty acid desaturase gene in methylotrophic yeast.


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