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J Biol Chem, Vol. 273, Issue 45, 29360-29366, November 6, 1998

Identification of 5-Desaturase from Mortierella alpina by Heterologous Expression in Bakers' Yeast and Canola

Deborah S. Knutzon, Jennifer M. Thurmond^§, Yung-Sheng Huang^§, Sunita Chaudhary^§, Emil G. Bobik Jr.^§, George M. Chan, Stephen J. Kirchner^§, and Pradip Mukerji^§

From the ^§ Ross Products Division, Abbott Laboratories, Columbus, Ohio 43215 and  Calgene, LLC, Davis, California 95616

A DNA fragment with homology to 6-desaturases from borage and cyanobacteria was isolated after polymerase chain reaction amplification of Mortierella alpina cDNA with oligonucleotide primers corresponding to the conserved regions of known 6-desaturase genes. This fragment was used as a probe to isolate a cDNA clone with an open reading frame encoding 446 amino acids from a M. alpina library. Expression of this open reading frame from an inducible promoter in Saccharomyces cerevisiae in the presence of various substrates revealed that the recombinant product had 5-desaturase activity. The effects of growth and induction conditions as well as host strain on activity of the recombinant 5-desaturase in S. cerevisiae were evaluated. Expression of the M. alpina 5-desaturase cDNA in transgenic canola seeds resulted in the production of taxoleic acid (5,9-18:2) and pinolenic acid (5,9,12-18:3), which are the 5-desaturation products of oleic and linoleic acids, respectively.

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