Plant Acyl-CoA:Lysophosphatidylcholine Acyltransferases (LPCATs) have different specificities in their forward and reverse reactions

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DOI	Resolve DOI: https://doi.org/10.1074/jbc.M113.521815
Author	Search for: Lager, Ida; Search for: Lindberg Yilmaz, Jenny; Search for: Zhou, Xue-Rong; Search for: Jasieniecka, Katarzyna; Search for: Kazachkov, Michael¹; Search for: Wang, Peng; Search for: Zou, Jitao¹; Search for: Weselake, Randall; Search for: Smith, Mark A.¹; Search for: Bayon, Shen; Search for: Dyer, John M.; Search for: Shockey, Jay M.; Search for: Heinz, Ernst; Search for: Green, Allan; Search for: Banas, Antoni; Search for: Stymne, Sten
Name affiliation	National Research Council Canada. Aquatic and Crop Resource Development
Format	Text
Type	Article
Journal title	The Journal of Biological Chemistry
ISSN	0021-9258 1083-351X
Volume	288
Issue	52
Pages	36902–36914
Abstract	Acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT) enzymes have central roles in acyl editing of phosphatidylcholine (PC). Plant LPCAT genes were expressed in yeast and characterized biochemically in microsomal preparations of the cells. Specificities for different acyl-CoAs were similar for seven LPCATs from five different species, including species accumulating hydroxylated acyl groups in their seed oil, with a preference for C18-unsaturated acyl-CoA and low activity with palmitoyl-CoA and ricinoleoyl (12-hydroxyoctadec-9-enoyl)-CoA. We showed that Arabidopsis LPCAT1 and LPCAT2 enzymes catalyzed the acylation and de-acylation of both sn positions of PC, with a preference for the sn-2 position. When acyl specificities of the Arabidopsis LPCATs were measured in the reverse reaction, sn-2-bound oleoyl, linoleoyl, and linolenoyl groups from PC were transferred to acyl-CoA to a similar extent. However, a ricinoleoyl group at the sn-2-position of PC was removed 4–6-fold faster than an oleoyl group in the reverse reaction, despite poor utilization in the forward reaction. The data presented, taken together with earlier published reports on in vivo lipid metabolism, support the hypothesis that plant LPCAT enzymes play an important role in regulating the acyl-CoA composition in plant cells by transferring polyunsaturated and hydroxy fatty acids produced on PC directly to the acyl-CoA pool for further metabolism or catabolism.
Publication date	2013-11-04
Publisher	American Society for Biochemistry and Molecular Biology
Language	English
Peer reviewed	Yes
NPARC number	23000588
Export citation	Export as RIS
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Record identifier	4673c77e-e816-4d49-adc9-511e33e07af1
Record created	2016-08-04
Record modified	2020-02-19

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Date modified:: 2020-02-23