Difference between revisions of "Part:BBa K4343105"

Revision as of 08:18, 9 October 2022

BgElo9

IgASE2 encodes ∆-9 elongase from Isochrysis galbana which functions in the Δ-9 elongase/desaturase pathway and could convert C18:2 to C20:2.

Characterization

Heterologous expression of IgASE2 could enable engineered Y. lipolytica to produce C20:2 fatty acids that couldn’t be produced in wild-type Y. lipolytica.

Literature

The IgASE2 contained a 786 bp ORF encoding a protein of 261 amino acids that shared 87% identity with the reported ∆-9-elongase IgASE1.

The coding sequence of IgASE2 contains a 786 bp ORF encoding a protein of 261 amino acids and has 87% homology to the reported ∆9-elongase IgASE1, a 44 bp 5' untranslated region and an 823 bp 3' untranslated region. The function of IgASE2 was demonstrated by heterologous expression in Saccharomyces cerevisiae. In S. cerevisiae, IgASE2 catalyzes the conversion of linoleic acid (LA, C18:2n-6) and α-linolenic (ALA, C18:3n-3) to eicosadienoic acid (EDA, C20:2n-6) and eicosatrienoic acid (ETrA, C20:3n-3), respectively.

Reference

Li, M., Ou, X., Yang, X., Guo, D., Qian, X., Xing, L., & Li, M. (2012). Cloning and identification of a novel C18-Δ9 polyunsaturated fatty acid specific elongase gene from DHA-producing Isochrysis galbana H29. Biotechnology and Bioprocess Engineering, 17(1), 22-32.

Sequence and Features