Defining the extreme substrate specificity of Euonymus alatus diacylglycerol acetyltransferase, an unusual membrane-bound O-acyltransferase

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dc.contributor.author Bansal, Sunil
dc.contributor.author Durrett, Timothy P.
dc.date.accessioned 2017-11-30T21:40:52Z
dc.date.available 2017-11-30T21:40:52Z
dc.identifier.uri http://hdl.handle.net/2097/38328
dc.description Citation: Bansal, S., & Durrett, T. P. (2016). Defining the extreme substrate specificity of Euonymus alatus diacylglycerol acetyltransferase, an unusual membrane-bound O-acyltransferase. Bioscience Reports, 36, 9. doi:10.1042/bsr20160277
dc.description.abstract Euonymus alatus diacylglycerol acetyltransferase (EaDAcT) synthesizes the unusually structured 3-acetyl-1,2-diacylglycerols (acetyl-TAG) found in the seeds of a few plant species. A member of the membrane-bound O-acyltransferase (MBOAT) family, EaDAcT transfers the acetyl group from acetyl-CoA to sn-1,2-diacylglycerol (DAG) to produce acetyl-TAG. In vitro assays demonstrated that the enzyme is also able to utilize butyryl-CoA and hexanoyl-CoA as acyl donors, though with much less efficiency compared with acetyl-CoA. Acyl-CoAs longer than eight carbons were not used by EaDAcT. This extreme substrate specificity of EaDAcT distinguishes it from all other MBOATs which typically catalyze the transfer of much longer acyl groups. In vitro selectivity experiments revealed that EaDAcT preferentially acetylated DAG molecules containing more double bonds over those with less. However, the enzyme was also able to acetylate saturated DAG containing medium chain fatty acids, albeit with less efficiency. Interestingly, EaDAcT could only acetylate the free hydroxyl group of sn-1,2-DAG but not the available hydroxyl groups in sn-1,3-DAG or in monoacylglycerols (MAG). Consistent with its similarity to the jojoba wax synthase, EaDAcT could acetylate fatty alcohols in vitro to produce alkyl acetates. Likewise, when coexpressed in yeast with a fatty acyl-CoA reductase capable of producing fatty alcohols, EaDAcT synthesized alkyl acetates although the efficiency of production was low. This improved understanding of EaDAcT specificity confirms that the enzyme preferentially utilizes acetyl-CoA to acetylate sn-1,2-DAGs and will be helpful in engineering the production of acetyl-TAG with improved functionality in transgenic plants.
dc.relation.uri https://doi.org/10.1042/bsr20160277
dc.rights Attribution 4.0 International (CC BY 4.0)
dc.rights.uri https://creativecommons.org/licenses/by/4.0/
dc.subject Acetyl-Tags
dc.subject Acetyltransferase
dc.subject Mboat
dc.subject Substrate Specificity
dc.subject Triacylglycerols
dc.subject Positional-Species Composition
dc.title Defining the extreme substrate specificity of Euonymus alatus diacylglycerol acetyltransferase, an unusual membrane-bound O-acyltransferase
dc.type Article
dc.date.published 2016
dc.citation.doi 10.1042/bsr20160277
dc.citation.issn 0144-8463
dc.citation.jtitle Bioscience Reports
dc.citation.spage 9
dc.citation.volume 36
dc.contributor.authoreid tdurrett
dc.contributor.kstate Durrett, Timothy P.


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