Isolation and Characterization of Δ6-Desaturase, an ELO-Like Enzyme and Δ5-Desaturase from the Liverwort Marchantia Polymorpha and Production of Arachidonic and Eicosapentaenoic Acids in the Methylotrophic Yeast Pichia Pastoris

Isolation and Characterization of Δ6-Desaturase, an ELO-Like Enzyme and Δ5-Desaturase from the... The liverwort Marchantia polymorpha contains high proportions of arachidonic and eicosapentaenoic acids. In general, these C20 polyunsaturated fatty acids (PUFA) are synthesized from linoleic and α-linolenic acids, respectively, by a series of reactions catalyzed by Δ6-desaturase, an ELO-like enzyme involved in Δ6 elongation and Δ5-desaturase. Here we report the isolation and characterization of the cDNAs, MpDES6, MpELO1 and MpDES5, coding for the respective enzymes from M. polymorpha. Co-expression of the MpDES6, MpELO1 and MpDES5 cDNAs resulted in the accumulation of arachidonic and eicosapentaenoic acids in the methylotrophic yeast Pichia pastoris. Interestingly, Δ6 desaturation by the expression of the MpDES6 cDNA appears to occur both in glycerolipids and the acyl-CoA pool, although other lower-plant Δ6-desaturases are known to have a strong preference for glycerolipids. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Isolation and Characterization of Δ6-Desaturase, an ELO-Like Enzyme and Δ5-Desaturase from the Liverwort Marchantia Polymorpha and Production of Arachidonic and Eicosapentaenoic Acids in the Methylotrophic Yeast Pichia Pastoris

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Publisher
Kluwer Academic Publishers
Copyright
Copyright © 2004 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1023/B:PLAN.0000036366.57794.ee
Publisher site
See Article on Publisher Site

Abstract

The liverwort Marchantia polymorpha contains high proportions of arachidonic and eicosapentaenoic acids. In general, these C20 polyunsaturated fatty acids (PUFA) are synthesized from linoleic and α-linolenic acids, respectively, by a series of reactions catalyzed by Δ6-desaturase, an ELO-like enzyme involved in Δ6 elongation and Δ5-desaturase. Here we report the isolation and characterization of the cDNAs, MpDES6, MpELO1 and MpDES5, coding for the respective enzymes from M. polymorpha. Co-expression of the MpDES6, MpELO1 and MpDES5 cDNAs resulted in the accumulation of arachidonic and eicosapentaenoic acids in the methylotrophic yeast Pichia pastoris. Interestingly, Δ6 desaturation by the expression of the MpDES6 cDNA appears to occur both in glycerolipids and the acyl-CoA pool, although other lower-plant Δ6-desaturases are known to have a strong preference for glycerolipids.

Journal

Plant Molecular BiologySpringer Journals

Published: Oct 10, 2004

References

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