Matches in SemOpenAlex for { <https://semopenalex.org/work/W2272391812> ?p ?o ?g. }
- W2272391812 abstract "A more sustainable access to alternative sources for very long chain polyunsaturated fatty acid (VLCPUFA) containing oils becomes more important as a human diet enriched in n-3 fatty is believed to have beneficial effects on human health. While most of the recently published studies focused successfully on the search for desaturases and elongases to reconstitute pathways for the biosynthesis of VLCPUFA, it is now of growing interest to explore additional enzymatic functions that are involved in the specific accumulation of VLCPUFA in transgenic oilseed crops. With respect to engineering oilseed crops as a source of VLCPUFA for human nutrition, the aim of the present study was to identify and to characterize acyltransferases with novel substrate specificities from microalgae and moss. These novel acyltransferases might be implemented in transgenic plants in order to enhance the biosynthetic capacity and accumulation of VLCPUFA, respectively. Genes encoding putative LPAAT, LPCAT, DGAT, and PDAT were identified in the genomes of the microalgae O. tauri, O. lucimarinus, and the moss P. patens. The genes were isolated and the enzymatic functions of the corresponding recombinant enzymes were characterized by complementation studies in different yeast mutant strains. It was shown that two putative LPAAT from M. squamata and P. patens do not participate in the acyl-exchange between the PtdCho-pool and acyl-CoA-pool. OlLPCAT, a novel LPCAT from O. lucimarinus , was shown to be able to optimize the interaction of lipid-dependent and CoA-dependent reaction steps in the course of transgenic biosynthesis of VLCPUFA in S. cerevisiae. Three putative members of the DGAT2 family of enzymes were isolated from O. tauri. Among these, OtDGAT2B displayed DGAT activity upon expression in yeast. The activity of OtDGAT2B exhibited a broad substrate specificity which might reflect the incorporation of a wide range of different fatty acids into storage lipids of O. tauri. Furthermore, a PDAT was isolated from O. tauri and characterized in yeast. OtPDAT exhibited a strict preference for polyunsaturated fatty acid substrates, thus saturated and monounsaturated fatty acid substrates were excluded from the formation of triacylglycerols. Although the interaction of OlLPCAT and OtPDAT with pathways for the production of VLCPUFA in transgenic oil seed crops still needs to be assessed, both acyltransferases possess promising activities to improve the accumulation of VLCPUFA in such plants." @default.
- W2272391812 created "2016-06-24" @default.
- W2272391812 creator A5020842159 @default.
- W2272391812 date "2009-12-04" @default.
- W2272391812 modified "2023-09-24" @default.
- W2272391812 title "Identifizierung und funktionale Charakterisierung neuartiger Acyltransferasen aus Mikroalgen" @default.
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