Plant Acyl-CoA:Lysophosphatidylcholine Acyltransferases (LPCATs) Have Different Specificities in Their Forward and Reverse Reactions

Authors

Ida Lager, Swedish University of Agricultural SciencesFollow
Jenny Lindberg Yilmaz, Biotechnology Research AB
Xue-Rong Zhou, CSIRO Food & Nutrition, Sydney, AustraliaFollow
Katarzyna Jasieniecka, University of Gdansk and Medical University of Gdansk
Michael Kazachkov, National Research Council of Canada, Saskatoon
Peng Wang, University of Nebraska-LincolnFollow
Jitao Zou, eNational Research Council of Canada, Saskatoon
Randall Weselake, University of Alberta, Edmonton
Mark A. Smith, eNational Research Council of Canada, SaskatoonFollow
Shen Bayon, State University, Pullman
John M. Dyer, United States Department of Agriculture-Agricultural Research Service, Maricopa
Jay Shockey, USDA-ARS, New OrleansFollow
Ernst Heinz, University of Hamburg
Allan Green, Commonwealth Scientific and Industrial Research Organisation Plant Industry
Antoni Banas, University of Gdansk and Medical University of Gdansk
Sten Stymne, Swedish University of Agricultural Sciences

Date of this Version

2014

Citation

THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 288, NO. 52, pp. 36902–36914, December 27, 2013

Comments

Published in the U.S.A.

Abstract

Background: Acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT) enzymes have central roles in acyl editing of phosphatidylcholine.

Results: Plant LPCATs were expressed in yeast and biochemically characterized.

Conclusion: LPCATs can edit acyl composition of phosphatidylcholine through their combined forward and reverse reactions.

Significance: Plant LPCATs play a role in editing both sn-positions of PC and remove ricinoleic acid with high selectivity from this lipid.