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Identification and functional expression of a type 2 acyl-CoA:diacylglycerol acyltransferase (DGAT2) in developing castor bean seeds which has high homology to the major triglyceride biosynthetic enzyme of fungi and animals

Kroon, Johan T.M.; Wei, Wenxue; Simon, William J.; Slabas, Antoni R.

Authors

Wenxue Wei

William J. Simon

Antoni R. Slabas



Abstract

Seed oil from castor bean (Ricinus communis) contains high amounts of hydroxy fatty acid rich triacylglycerols (TAGs) that can serve as raw material for production of bio-based products such as nylon, cosmetics, lubricants, foams, and surfactants. Diacylglycerol acyltransferase (DGAT) catalyses the terminal reaction in the acyl-CoA dependent Kennedy pathway of triglyceride biosynthesis. There is still some debate whether there are three or four enzymes in yeast that have DGAT activity and catalyse the synthesis of TAG but of these the DGAT2 homologue Dga1 contributes in a major way to TAG biosynthesis. Here we report on the cloning of a cDNA for DGAT2 from castor bean and prove its biological activity following expression in yeast and enzymatic assays using diricinolein as the acceptor and ricinoleoyl-CoA as the donor. Previous reports of DGAT in castor have focussed on DGAT1 which has little amino acid sequence homology to DGAT2. Expressional studies demonstrate that DGAT2 is 18-fold more highly expressed in seeds than in leaves and shows temporal specific expression during seed development. In contrast, DGAT1 shows little difference in expression in seeds versus leaves. We conclude that in castor bean DGAT2 is more likely to play a major role in seed TAG biosynthesis than DGAT1.

Citation

Kroon, J. T., Wei, W., Simon, W. J., & Slabas, A. R. (2006). Identification and functional expression of a type 2 acyl-CoA:diacylglycerol acyltransferase (DGAT2) in developing castor bean seeds which has high homology to the major triglyceride biosynthetic enzyme of fungi and animals. Phytochemistry, 67(23), 2541-2549. https://doi.org/10.1016/j.phytochem.2006.09.020

Journal Article Type Article
Acceptance Date Sep 18, 2006
Online Publication Date Nov 7, 2006
Publication Date Dec 31, 2006
Deposit Date Sep 9, 2021
Journal Phytochemistry
Print ISSN 0031-9422
Publisher Elsevier
Volume 67
Issue 23
Pages 2541-2549
DOI https://doi.org/10.1016/j.phytochem.2006.09.020
Public URL https://durham-repository.worktribe.com/output/1251158